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1. Introduction
Microbial infections contribute substantially to global mortality trends. Antibiotic resistance is one of the biggest challenges for the clinical sector, industry, environment, and societal development. Unfortunately, the emergence of drug-resistant pathogens is rapidly growing, and the world is heading toward the post-antibiotic era [1, 2]. Bacteria possess three defined types of antimicrobial resistance: intrinsic, acquired, and phenotypic or adaptive resistance [3, 4, 5, 6, 7, 8, 9, 10, 11]. Although there are multiple causes of the resistance phenomenon, it is considered that antimicrobial resistance is an old natural phenomenon when microbes are exposed to antimicrobial drugs, with an accelerated evolution triggered not only by the abusive use of antibiotics but also such as wrong choices, inadequate dosing, and poor adherence to treatment guidelines that contribute to the increasing antimicrobial resistance selection [12, 13]. In addition, antibiotic treatment for difficult-to-treat multidrug-resistant bacterial infections is limited [13]. ESKAPE pathogens (Enterococcus faecium, Staphylococcus aureus, Klebsiella pneumoniae, A. baumannii, Pseudomonas aeruginosa, Enterobacter species) are among the most common opportunistic pathogens in nosocomial infections [14]. The abbreviation ESKAPE reflects the ability of these organisms to “escape” killing by antibiotics and defy eradication by conventional therapies, which accounts for increased morbidity and mortality for improved resource utilization in healthcare [15]. One of the ESKCAPE pathogens responsible for nosocomial and community-acquired infections is A. baumannii, a Gram-negative, non-motile, non-fermentative, and non-sporulated bacterium Moraxellaceae family [16] that is part of the Acinetobacter calcoaceticus–A. baumannii complex (Acb). Currently, six species, namely A. calcoaceticus, A. baumannii, A. pittii, A. nosocomialis, A. seifertii, and A. lactucae (a later heterotypic synonym of A. dijkshoorniae) [17, 18], belonging to the Acb complex have been associated with human diseases [19]. Even though these species differ in antimicrobial resistance, pathogenicity, and epidemiology [20], the Acb complex is genetically and physiologically highly related, making it difficult to distinguish them phenotypically with standard laboratory methods [21]. Of all the species in the Acb complex, A. baumannii is the most widespread in hospitals, even associated with an increased risk of morbidity, mortality, high treatment costs, and long periods of hospitalization [22]. A. baumannii causes various infections, including wounds, skin, urinary tract infections, pneumonia, meningitis, and bacteremia [23, 24]. There are several nomenclatures in the literature based on the number of resistance classes of antibiotics. According to Magiorakos et al. (2012), a multidrug-resistant (MDR) strain is resistant to at least one antimicrobial in more than three classes of antimicrobials; and extensively drug-resistant (XDR) strain is one resistant to at least one antimicrobial in all classes of antimicrobials except two or fewer types, and a pan drug-resistant (PDR) strain is resistant to all antimicrobial agents [25]. A. baumannii has globally emerged as a highly troublesome nosocomial pathogen revealing MDR, XDR, and PDR phenotypes, and unfortunately, evidence has shown an increased A. baumannii antibiotic resistance over time [26]. A. baumannii is one of the most critical and fearful pathogens with treatment options limited due to many aspects: its extended virolome and resistome, evasion of the host’s immune effectors, ability to survive in extreme environmental conditions, to grow in biofilms, and to switch to latent growth forms with a minimal metabolic rate [27, 28]. The World Health Organization (WHO) has recently published a report, which also highlighted A. baumannii resistant to carbapenems (CRAb) [29, 31] which was classified in the group of “priority 1 for research and develop new antibiotic treatments” and was considered as a “critical” pathogen [31]. One of the antimicrobial agents with high potential for research and development of anti-Acinetobacter drugs is the antimicrobial peptides [32]. This chapter aimed to review the powerful antimicrobial peptides described with activity against A. baumannii multiresistant.
2. Antimicrobial peptides
Antimicrobial peptides (AMPs) may represent an alternative to current antibiotics in MDR A. baumannii ESKAPE pathogen [33]. AMPs (also known as host defense peptides) are small polycationic peptides naturally produced by living organisms with both microbicidal and immunomodulatory activities, acting as a primary barrier against pathogens, including protozoa, víruses, bacteria, archaea, fungi, plants, and animals as a part of innate immunity system [34, 35, 36, 37, 38, 39, 40, 41]. However, the computational design of synthetic AMPs with improved activity is also being developed [42]. They interact with cell membrane through electrostatic interactions, causing the inhibition of protein and nucleic acid synthesis and final cellular lysis by apoptosis and necrosis [43, 44]. In addition to the antimicrobial properties, some AMPs have other activities, such as anticancer antioxidant, wound healing, immunoregulatory [38, 45, 46]. AMPs also play an essential role in regulating immune processes such as activating and recruiting immune system cells, angiogenesis, and inflammation [47]. AMPs are amphipathic molecules with a positive electric charge, varying molecular weight, and containing about 11–50 amino acid residues [47, 48]. AMPs are classified into α-helical, β-sheet, and extended peptide families [49, 50, 51] and interact with the membranes initially through electrostatic and hydrophobic interactions (Figure 1), accumulating at the surface and self-assemble on the bacterial membrane after reaching a particular concentration [52, 53].
Figure 1.
Interaction of cationic AMPs with eukaryotic and bacterial membranes. Images were created using BioRender.com.
At this stage, various models have been proposed to describe the action of AMPs. The models can be classified under two broad categories: transmembrane pore (TMP) and non-pore models (NPM), and the TMP can be further subdivided into the barrel-stave pore and toroidal pore models. In the barrel-stave model, the AMPs are initially oriented parallel to the membrane but eventually insert perpendicularly in the lipid bilayer [54] (Figure 2A), thus promoting lateral peptide-peptide interactions, like that of membrane protein ion channels. Peptide amphipathic structure (α and/or β sheet) is essential in this pore formation mechanism as the hydrophobic regions interact with the membrane lipids and hydrophilic residues from the lumen of the channels [55, 56]. A unique property associated with AMPs in this category is a minimum length of ∼22 residues (α helical) or ∼ 8 residues (β sheet) to span the lipid bilayer. Only a few AMPs, such as alamethicin [57], pardaxin [58, 59], and protegrins [55], have been shown to form barrel stave channels.
Figure 2.
Mechanisms of action of AMPs in bacteria. A) Barrel-stave model: AMPs stack into the bilayer of the cell membrane to form a channel. (B) Toroidal pore model: Accumulation of vertically and bend embedded AMPs in the cell membrane to form a pore structure, (C) carpet model: Distribution of AMPs on membrane surface that evolve to detergent-like mode, forming micelles, (D) images were created using BioRender.com.
Furthermore, in the toroidal pore model, the peptides also insert perpendicularly in the lipid bilayer, but specific peptide-peptide interactions are not present [57]. Instead, the peptides induce a local curvature of the lipid bilayer with the pores partly formed by peptides and partly by the phospholipid head group (Figure 2B). Thus, the dynamic and transient lipid-peptide supramolecule is known as the “toroidal pore.” The distinguishing feature of this model compared to the barrel-stave pore is the net arrangement of the bilayer. In the barrel-stave pore, the hydrophobic and hydrophilic sequence of the lipids is maintained, whereas, in toroidal pores, the hydrophobic and hydrophilic arrangement of the bilayer is disrupted, thus providing alternate surfaces for the lipid tail and the lipid head group to interact with. Furthermore, as the pores are transient upon disintegration, some peptides translocate to the inner cytoplasmic leaflet entering the cytoplasm and potentially targeting intracellular components [60]. Other features of the toroidal pore include ion selectivity and discrete size [61]. Several AMPs such as magainin 2 [62], lacticin Q [62], aurein 2.2 [63], and melittin [57, 62] have been shown to form toroidal pores. In addition, the type of pore started by aurein 2.2 has been shown to depend on the lipid composition: In a 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC)/1-palmitoyl-2-oleoyl-sn-glycerol-3-phospho-(1′-rac-glycerol) POPG (1:1) membrane model, the peptides induce toroidal pores, whereas in a 1,2-dimyristoyl-sn-glycerol-3-phosphocholine (DMPC)/1,2-dimyristoyl-sn-glycero-3-phospho-(1′-rac-glycerol) DMPG (1,1) membrane model, the peptides work in a detergent-like model (details below) indicating the importance of the hydrophobic thickness of the lipid bilayer and the membrane composition [64, 65]. Ultimately, both pore-forming models (toroidal pore and barrel) lead to membrane depolarization and eventually cell death.
AMPs can also act without forming specific pores in the membrane. One of these models is designated as the carpet model [61, 62, 66]. In this case, the AMPs adsorb parallel to the lipid bilayer and reach a threshold concentration to cover the surface of the membrane, thereby forming a “carpet” (Figure 2C) and leading to unfavorable interactions on the membrane surface. Consequently, the membrane integrity is lost, producing a detergent-like effect, which eventually disintegrates the membrane by forming micelles. The final collapse of the membrane bilayer structure into micelles is the detergent-like model (Figure 2D). The carpet model does not require specific peptide-peptide interactions of the membrane-bound peptide monomers; it also does not require the peptide to insert into the hydrophobic core to form transmembrane channels or specific peptide structures [67]. Many peptides act as antimicrobial agents despite their specific amino acid composition or the length of the sequence. Such AMPs typically act using the carpet model [66] at high concentrations because of their amphiphilic nature. Examples of AMPs acting by the carpet model are cecropin [68], indolicidin [69], aurein 1.2 [67], and LL-37 [66].
Overall, there are many models to describe the MOA of AMPs. In addition to those given above, other related models include the interfacial activity model, the electroporation model, and the Shai-Huang-Matsazuki model [62]. Some models do not make the specific distinctions shown in Figure 2. For example, it has been suggested that the carpet-like mechanism is a prerequisite step for the toroidal pore model [62]. Most studies to elucidate the MOA of AMPs involve the use of model membranes. The mode of action of only a few AMPs has been investigated with whole bacterial cells using imaging techniques [70, 71]. Different results may be obtained using other membrane models or assay conditions; for example, more than one MOA is possible for certain AMPs such as BP100 as the peptide-to-lipid ratio changes [72], indicating that the models described here may or may not translate directly to what is occurring in bacteria.
An online antimicrobial peptide database, APD3, list examples of AMPs, including both synthetically synthesized and compounds produced by living organisms [37]. In addition, many AMPs are currently being studied to elucidate their therapeutic efficacy against A. baumannii strains (Table 1).
NA, not available; AH, alpha helical; IPM, imipenem; COL, colistin.
2.1 Cathelicidins
Cathelicidins are a group of cationic AMPs (CAMPs) (with more than 30 members) detected in the immune system of some vertebrates that have in their structure two domains involved in antimicrobial activity [145]. Compared with carbapenems (imipenem and meropenem), which are considered the drugs of choice for infections caused by MDR A. baumannii (MIC = 16–32 mg/L) [146], these peptides exhibit excellent activity.
2.1.1 LL-37
The most studied member of the cathelicidins family is LL-37 (Human cathelicidin) with an α-helical structure. It is produced by many cell types as a part of innate immunity and exhibits broad-spectrum microbicidal activities against Gram-positive and Gram-negative bacteria by plasma-membrane disruption [147]. Other properties were also described, like immunomodulation properties such as chemoattraction and activation of various immune cells, neutralizing the lipopolysaccharide (LPS), regulating the inflammatory response, wound closure, and chemotaxis [38, 148, 149, 150, 151]. Feng et al. Investigated the anti-A. baumannii activity of LL-37 and fragments KS-30 and KR-12 against one sensitive and four MDR A. baumannii clinical isolates [73]. The minimum inhibitory concentration (MIC) for three pieces of KS-30, KR-20, and KR-12 was 8–16, 16–64, and 128–256 μg/ml, respectively. At the same time, LL-37 inhibited all sensitive and drug-resistant strains at the concentration of 16–32 μg/ml. Furthermore, LL-37 and the fragment KS-30 have been found to significantly inhibited and dispersed the A. baumannii biofilm in abiotic surfaces at 32 and 64 μg/ml, respectively [73]. A panel of synthetic peptides based on human LL-37 AMP shows potent microbicidal activity against several ESKAPE pathogens without selecting resistance and can also eliminate persister cells and biofilms of P. aeruginosa, A. baumannii, and S. aureus in the micromolar scale [74]. SAAP-148 is an α-helical AMP, able to suppress MDR A. baumannii without causing resistance and prevents biofilm formation. Studies showed that this peptide could inhibit the growth of A. baumannii MDR at a concentration of 6 μg/m. Treatment with this peptide (animal model) appointment has been shown to eliminate acute and biofilm-related infections by A. baumannii in an ex vivo human skin infection model and an in vivo murine skin infection model at concentrations above 5% [74].
2.1.2 Snake cathelicidins
The anti-A. baumannii activity among the cathelicidins isolated from snakes has been reported for the peptides cathelicidin-BF (Cath-BF) [75] and Naja atra cathelicidin (NA-CATH). One of the best-known cathelicidins is Cath-BF having an α-helical structure, isolated from the venous glands of the species Bungatus fasciatus [152]. It has been shown that Cath-BF causes bacterial death through two bacterial membrane disruption mechanisms and attacking intracellular targets [152]. According to available reports, this peptide is highly active against drug-resistant clinical isolates of A. baumannii, inhibiting its growth around 12.8 μg/ml concentration [75]. ZY4 cathelicidin-BF-15 derived, a cyclic peptide stabilized by a disulfide bridge with high stability in vivo (the half-life is 1.8 h), showed excellent activity against A. baumannii, including standard clinical MDR strains with MIC values ranging between 4.6 and 9.4 μg/mL. ZY4 killed bacteria by permeabilizing the bacterial membrane showed a low propensity to induce resistance, exhibited biofilm inhibition and eradication activities, and killed persister cells [76]. The peptide NA-CATH, produced by a cobra called N. atra, possesses an α-helical structure at N-terminal and an unstructured segment at C-terminal [77, 153]. This peptide exerts antimicrobial activity through the membrane lysis by membrane thinning or transient pore formation [154] and is highly active against drug-resistant and sensitive A. baumannii strains, completely inhibiting bacterial growth at a concentration of 10 μg/ml [77, 153]. In 2018, Zhao et al. identified a novel cathelicidin (OH-CATH) from the king cobra, with its analog DOH-CATH30 found to exhibit potent microbicidal activity (MIC 1.56 to 12.5 μg/mL) against several Gram-negative and Gram-positive bacteria, including MDR A. baumannii [78]. Other cathelicidins with antimicrobial activity, identified in the venous glands, are OH-CATH30, from the venom of the cobra and mirtoxin, from Myrmecia pilosula [78, 79], presenting antimicrobial activity through inhibition of planktonic bacterial growth and biofilm, eradication of persistent bacterial cells, and inhibition of inflammatory process [76, 78].
Compounds with similar activity have been identified in the venom of some scorpion species and tested against antibiotic-resistant bacteria. Therefore, Al-Asmari et al. evaluate the in vitro antimicrobial activities of the toxins extracted from three medically necessary Saudi Scorpions. Among these, only Leiurus quinquestriatus showed significant broad-spectrum antimicrobial activity in a dose-dependent manner from 5 to 20 mg/mL, inhibiting 50.6% of growth and survival of MDR A. baumannii [80]. High antimicrobial activity was also observed for AMPs ranalexin and danalexin obtained from Rana catesbeiana [81], LS-sarcotoxin, and LS-stomoxyn (Lucilla serricata) [82], and minibactenecins (Capra hircus) [83]. However, further in vivo studies are needed to improve the pharmacokinetics of systemic administration and find solutions to avoid their degradation by proteases despite the antimicrobial activity on A. baumannii strains of these compounds.
2.1.3 Alligator cathelicidins
Alligator mississippiensis (American alligator), a member of order Crocodilia, lives in bacteria-laden environments but cannot often succumb to bacterial infections. Serum of alligators has antibacterial activity beyond that of human sérum [155], killing a wide range of pathogens, and it is believed that this activity is attributable at least partially to the presence of CAMPs in the alligator plasma and extracts [156]. A study by Barksdale et al. (2017) reported the anti-A. baumannii effect of AMPs produced by American alligator: cathelicidin called AM-CATH36 and its two fragments including AM-CATH28 and AM-CATH21 [77]. Alligator cathelicidin can inhibit the growth of both drug-resistant and sensitive A. baumannii at the 2.5 μg/ml concentration. Furthermore, two shorter fragments of this peptide can inhibit the drug-resistant A. baumannii at a 10 μg/ml concentration. The anti-A. baumannii effect of these three peptides is through membrane permeabilization. Interestingly, MDR clinical isolates of A. baumannii were more susceptible to both the AM CATH21 and AM-CATH28 peptides than the sensitive strains.
2.1.4 Wallaby antimicrobial
The marsupial AMP Wallaby antimicrobial 1 (WAM-1) is a cathelicidin isolated from the mammary gland of the Tammar wallaby (Macropus eugenii) with antibacterial and antifungal activities with high potential to combat drug-resistant pathogens [84, 157]. Spencer et al. (2018) studied the AMP LL-37 and WARM-1 effects on MDR A. baumannii, and both peptides were able to inhibit biofilm formation in all clinical isolates at some concentrations of WAM-1 effectively dispersed 24-h biofilms in most isolates tested, including MDR strains [85]. The antibacterial effects of LL-37are diminished in the presence of human serum. However, this is not the case with WAM-1. Although the mechanism of action has yet to be determined, WAM-1 has been shown in vitro to be 12 to 80 times more effective than LL-37 in its ability to kill several bacterial pathogens, including several clinical isolates of A. baumannii. Unlike LL-37, WAM-1 is not inhibited by high NaCl concentrations and does not cause hemolysis in human red blood cells (RBC), so it has the potential to be used for in vivo applications [85].
2.1.5 Bovine cathelicidins (Indolicidin and Bactenecin)
Indolicidin is a short tryptophan-rich cationic AMP encoded by a member of the cathelicidin gene family, isolated from cytoplasmic granules of the bovine neutrophils [158, 159]. Indolicidin acts by displacing divalent cations from their binding sites on the surface of the cell membrane and causes bacterial death through channel formation in the cytoplasmic membrane [88]. Indolicidin not only forms pores in the membrane but can also inhibit DNA processing enzymes [160, 161]. This peptide is among the potent anti-A. baumannii AMPs with MIC of 4–32 and 16 μg/ml against sensitive and colistin-resistant clinical isolates, respectively [86]. In a study by Giacometti et al. were investigated the in vitro activity of indolicidin and other AMPs alone and in combination with antimicrobial agents, the MIC of indolicidin against 12 MDR clinical isolates was reported as 2–64 μg/ml [87]. Isolated from bovine, ovine, and caprine neutrophil granules, Bactenecin is a short cyclic, arginine-rich cationic AMP [89] with a type I β-turn structure and forms a loop due to the disulfide bond between cysteines 3 and 11 [90]. These AMPs act by permeabilizing the cell membrane and inhibiting protein and RNA synthesis in bacteria [70]. Vila-Farres et al. (2012) reported the anti-A. baumannii effect of this peptide can inhibit sensitive and colistin-resistant strains of A. baumannii at 16 and 64 μg/ml, respectively [86].
2.2 Defensins
Defensins are an evolutionarily ancient class of AMPs present in animals, plants, and fungi involved in the immune system of living organisms and contain six (invertebrates) to eight conserved cysteine residues in their structure. They are categorized into three subfamilies of α, β, and θ-defensins [162]. Most defensins bind to the cell membrane and make pores, leading to bacterial death [163].
2.2.1 α-Defensins (HNPs and HD5)
The subfamily of human neutrophil peptides (HNPs), also known as α-defensins, are secreted and released from polymorphonuclear neutrophil (PMN) granules upon activation and are conventionally involved in microbial killing [164]. Two important CAMPs HNP-1 and HNP-2, which differ in only one initial amino acid, can inhibit the growth of the standard strain of A. baumannii ATCC 19606 at a concentration of 50 μg/ml. Interestingly, the colistin-resistant mutant of A. baumannii ATCC 19606 is much more sensitive (MIC = 3.25 μg/ml) to HNP-1 than the standard strain [86]. Human defensin 5 (HD5) has a relatively low anti-A. baumannii effect (MIC = 320 μg/ml). However, an analog called HD5d5 obtained by sequence modification presented a stronger bactericidal effect (MIC = 40 μg / ml) against A. baumannii, exerting the effect through damage to the membrane, accumulation in the cytoplasm, and reduction of catalase and superoxide dismutase activities [165, 166].
2.2.2 β-Defensins
Human β-Defensin (HBD) 2, 3 of this subfamily have anti-Acinetobacter effects. HBD-2 is primarily produced by the epithelial lining of the respiratory and urinary tracts, and engaging is more effective on MDR clinical isolates than non-MDR isolates [167]. Longer than most of the natural AMPs, HBD-3 combined helix and β structure [147]. Even though the anti-Acinetobacter bactericidal effect is inhibited by exposure to human serum, it can kill all MDR and non-MDR A. baumannii clinical isolates at 4 μg/ml during 1.5 h in the serum-free environment. Thus, this peptide has the potential to be further studied for wounds infected by A. baumannii since it demonstrated wound-healing effects [97, 168].
2.2.3 α-Helical and antiparallel β-sheet defensins
CL-defensin, belonging to the family of insect defensins, is predicted to have a characteristic N-terminal loop, an α-helix, and an antiparallel β-sheet, which was supported by circular dichroism spectroscopy [95]. In addition, this peptide induces pore formation in other Gram-positive bacteria and causes a small amount of membrane permeabilization in A. baumannii [95].
2.3 Frog antimicrobial peptides
2.3.1 Magainin and pexiganan (its analog)
The Magainin-1 and 2 are cationic, α-helical, and amphipathic AMPs ionophores isolated from the skin of the African clawed frog (Xenopus laevis) [168, 169]. The primary mechanism of antimicrobial activity is probably pore formation in outer and inner membranes, although the exact mechanism of action is not yet precise [98, 170]. Despite both have anti-Acinetobacter training, Magainin-2 is much stronger and able to inhibit the growth of sensitive and MDR strains of A. baumannii at 4.9–64 μg/ml, while reported as 256 μg/ml for Magainin-1 [86, 98]. Magainin-2 has some advantages, such as anticancer effect, stability at physiological salt concentrations, lack of hemolytic activity, and toxicity for mammalian cells [98]. Furthermore, Magainin-2 can inhibit and eliminate the biofilm of A. baumannii [98]. Pexiganan AMP or MSI-78 is a synthetic analog of Magainin-2 with a potent and broad spectrum of action [171, 172]; it kills bacteria by forming toroidal pores in their cell membranes [172, 173]. Several studies have been performed on anti-Acinetobacter activity due to its being highly active against Acinetobacter. Pexiganan can inhibit the growth of MDR and sensitive clinical isolates of A. baumannii at a concentration of 1–8 μg/ml [100, 101, 174]. Jáskiewicz et al. studied the antimicrobial activity of eight peptides on A. baumannii ATCC 19606 reference strains. Among these, CAMEL and pexiganan showed potent antimicrobial and anti-biofilm activity [102].
2.3.2 Brevinin-2 related peptide (B2RP)
B2RP is an α-helical AMP isolated from the skin secretions of the mink frog Rana septentrionalis [175] and carpenter frog Rana virgatipes [176]. This peptide forms an α-helical structure adjacent to the target cell, resulting in the perturbation of the phospholipid bilayer that may lead to growth inhibition of bacterial death, and the application of this peptide for systemic use is limited due to the moderate toxicity for human red blood cells [177]. B2RP inhibited the growth of a susceptible strain of A. baumannii at 29 μg/ml concentration but inhibited the MDR isolates more efficiently at 7–13.9 μg/ml [103]. The analogs of these peptides (D4K, K16A, L18K) resulted in twofolds higher anti-A. baumannii activity and much lower hemolytic activity [103]. A study reported that the analog of B2RP with D4K substitution inhibited sensitive and colistin-resistant [103] and XDR isolates of A. baumannii [105].
2.3.3 B2RP-ERa
B2RP-ERa is a cationic AMP from the Brevinin family isolated from the skin of the Asian frog Hylarana erythraea [106, 178]. Shorter and with lower molecular weight, B2RP-ERa is structurally similar to B2RP. B2RP-ERa is an anti-inflammatory peptide with no toxic effect on peripheral blood mononuclear cells [179] with low hemolytic activity [178], which could inhibit the growth of sensitive and drug-resistant Acinetobacter strains at 8–32 and 8–64 μg/ml, respectively [104, 106].
2.3.4 Alyteserins
Alyteserins are a class of cationic AMPs, which firstly reported their presence in norepinephrine-stimulated skin secretions of the midwife toad [180]. However, initial studies show that Alyteserin-1c has more significant inhibitory activity against Gram-negative bacteria, while Alyteserin-2a is more active against Gram-positive bacteria [180], the anti-A. baumannii effects of these Alyteserins have already been proven [107, 108]. Alyteserin-1c is a cationic α-helical AMP with low hemolytic activity on human red blood cells firstly isolated from Alytes obstetricans [107, 180, 181]. The MIC and MBC against clinical isolates of MDR A. baumannii have been reported as 11.3–22.6 μg/ml [107]. Substitution of E4K on this AMP reduced the hemolytic activity, and enhanced the antimicrobial and cationic activity [107]. The analog [E4K] inhibits the growth of colistin-sensitive, colistin-resistant, and XDR A. baumannii isolates at concentrations of 4–16 μg/ml, 4–16 μg/ml [104], and 8–64 μg/ml, respectively [105]. Alyteserin-2a is also a tiny α-helical AMP that displays relatively weak antimicrobial and hemolytic activities. Despite its anti-A. baumannii potential was not high mainly, some structural changes resulted in lower toxicity against human erythrocytes and higher bactericidal effect (4–8 folds) against MDR isolates with MIC of 6.8–13.6 μg/ml [108].
2.3.5 Peptide glycine-leucine-amide
AM1 (PGLa-AM1) PGLa-AM1 is another Anti-Acinetobacter AMP isolated from the frog Xenopus amieti. In addition to the low hemolytic activity, it is also active against other pathogens, including E. coli and S. aureus [104, 106, 109], and can kill sensitive and colistin-resistant A. baumannii isolates at 16–128 μg/ ml concentration [104].
2.3.6 Caerulein precursor fragment (CPF)
CPF-AM1 is a cationic AMP firstly isolated from X. amieti [110]. This peptide is capable of bacterial binding LPS and has activity against Gram-negative and Gram-positive bacteria, primarily oral and respiratory pathogens, with advantages such as low hemolytic activity and lack of toxicity against fibroblast cells [109]. This anti-A. baumannii peptide inhibits the growth of sensitive and colistin-resistant strains at 16–128 and 4–128 μg/ml, respectively [104, 114]. CPF-B1, isolated from Marsabit clawed frog Xenopus borealis, is another anti-A. baumannii member of this family with low hemolytic activity. This peptide inhibits MDR A. baumannii clinical isolates at concentrations of 11.4–22.8 μg/ml [112]. Finally, CPF-C1 is a peptide member of this family with proved anti-A. baumannii effect with inhibitory activity against the strain at 5 μg/ml concentration [111].
2.3.7 Hymenochirins
Hymenochirins are a class of AMPs produced by two frogs of Pseudhymenochirus merlini and Hymenochirus boettgeri with letters P and B in the second part name of these peptides indicating the producing species of the peptide, respectively [37, 182]. Hymenochirin-1B is a cationic, α-helical amphibian host-defense peptide with antimicrobial, anticancer, and immunomodulatory properties. This peptide has anti-A. baumannii properties against MDR isolates with MIC of 19.1 μg/ml [113]. Among the analogs of hymenochirin-1B obtained by amino acid substitution method, [E6k and D9k] hymenochirin-1B reduced human erythrocytes’ toxicity and showed 3.9-folds higher activity against A. baumannii. [E6k and D9k] hymenochirin-1B is active against both MDR and XDR isolates and could inhibit the growth of these isolates at 4.9 μg/ml concentration [113]. Hymenochirin-1 Pa is another cationic member of this family with moderate hemolytic activity. This peptide inhibited the growth of XDR A. baumannii isolates at 7.5–15 μg/ml concentration [114, 182].
2.3.8 XT-7
XT-7 was first isolated from norepinephrine-stimulated skin secretions of Xenopus tropicalis [183]. The activity anti-Acinetobacteof this peptide was first reported against A. baumannii Euroclone I NM8 strain (MIC = 22.2 μg/ml) [111]. Later, the amino acid substitution of lysine at position 4 [G4K] increased the therapeutic index [115] principally. Subsequent studies were based on this new analog that inhibited sensitive and drug-resistant A. baumannii strains at concentrations of 4–32 and 4–64 μg/ml, respectively [104].
2.3.9 Buforins
Buforin II is a potent antimicrobial peptide derived from Burforin I, isolated from the stomach tissue of the Asian toad Bufo gargarizans [184]. It causes bacterial death by crossing the membrane, binding to intracellular targets, including DNA and RNA, and inhibiting cellular functions [116]. This peptide has a potent anti-Acinetobacter activity since it can hinder the growth of both sensitive and resistant isolates of A. baumannii at concentrations of 0.25–39 μg/ml [87, 98]. Buforin II alone or in combination with an antibiotic showed highly potent on A. baumannii sepsis treatment in a rat model [104].
2.4 Melittin
Melittin is a cationic amphipathic α-helical AMP isolated from the venom (approximately 50% of the dry weight) of the European honeybee (Apis mellifera) [185] with numerous reported properties such as antifungal [186], antiparasitic [187], antibacterial [185], antiviral, and anticancer properties [188]. The primary mechanism of melittin action is the membrane lysis through pore formation (a carpet-like mechanism) [189]. This potent anti-Acinetobacter peptide inhibits MDR and XDR clinical isolates at 0.125–2 μg/ml concentration [118, 119]. A study demonstrated that topical administration of melittin at concentrations of 16 and 32 μg/mL in mice killed 93.3% and 100% of an XDR A. baumannii on a third-degree burned area, respectively [118]. No toxicity was observed on the injured or healthy derma and circulating red blood cells in the examined mice. Recently, a study that evaluated the melittin against Brazilian clinical strains revealed that most strains were susceptible, except for one pan drug-resistant strain [190].
2.5 Cecropins
Cecropins, the lytic peptides, were initially isolated from the hemolymph of the giant silk moth, Hyalophora cecropia, and possess antibacterial and anticancer activity in vitro [191, 192]. The primary antimicrobial mechanism of cecropins is membrane lysis [193]. Cecropin A is a cationic amphipathic α-helical AMP that can induce apoptosis by oxidative stress in addition to attacking the membrane [194]. This peptide has potent antimicrobial activity against A. baumannii, inhibiting MDR clinical isolates at 0.5–32 μg/ml [99]. Vila-Farres et al. reported that this peptide inhibited the growth of sensitive and colistin-resistant strains of A. baumannii at 32 and 256 μg/ ml, respectively [86]. A pilot study that evaluated the viability of Caenorhabditis elegans infected by A. baumannii in the presence of 68 insect-derived AMPs identified 15 cecropin or cecropin-like peptides that prolonged the survival of worms infected with A. baumannii [121]. Interestingly, the direct investigation of the anti-Acinetobacter effect also showed that these 15 AMPs could inhibit the growth of A. baumannii at 4.5 to over 20 μg/ml concentrations. BR003-cecropin A, isolated from Aedes aegypti, is the most active member of this group. This peptide inhibited sensitive and MDR A. baumannii strains at 4.5 μg/ml [100]. Musca domestica cecropin (Mdc) isolated from the larvae of a housefly inhibits both standard (ATCC 19606) and MDR strains of A. baumannii at 4 μg/ml with high speed (half an hour) [122]. Cecropin P1, an AMP isolated from Ascaris suum of pig intestine, showed high activity against colistin-sensitive A. baumannii with MIC at 1.6 μg/ml. In contrast, there was less activity against the colistin-resistant strains with MIC >25 μg/ml [86].
Other peptides that showed great activity against susceptible MDR and extensively drug-resistant (XDR) A. baumannii strains were Cecropin-4, an α-helical synthetic AMP [124], and CAMEL, a hybrid AMP consisting of cecropin from H. cecropia and melittin from Apis melífera [102]. In addition, AMPs with activity against biofilms have been observed in cecropins identified in M. domestica [124], myxinidin isolated from Myxine glutinosa [104], and in the naturally occurring AMP complex isolated from the maggots of blowfly Calliphora vicina (Diptera, Calliphoridae) named FLIP7 (Fly Larvae Immune Peptides 7) [126].
2.6 Mastoparan
Mastoparan is a small cationic amphipathic α-helical AMP isolated from the hornet venom of Vespula lewisii [195, 196] with a robust anti-Acinetobacter activity. However, the anti-acinetobacter solid activity, the high hemolytic activity, and toxic effects affected highly therapeutic applications [197]. Mastoparan inhibited the growth of a sensitive wild-type A. baumannii ATCC 19606 and a colistin-resistant A. baumannii ATCC 19606 mutant at 4 and 1 μg/ml, respectively. This study also used 14 colistin-susceptible A. baumannii clinical isolates and 13 pan-resistant A. baumannii strains isolated in a hospital outbreak [198] and reported the MIC of 1–16 and 2–8 μg/ ml for sensitive and colistin-resistant isolates, respectively [86]. Mastoparan-AF (MP-AF), isolated from the hornet venom of Vespa affinis, also showed effective antimicrobial activity with MICs ranging from 2 to 16 μg/ml against MDR A. baumannii isolates [129]. Analogs of mastoparan were made to increase the stability of the peptide in serum. These analogs had an equal inhibitory effect with mastoparan against XDR A. baumannii strains (4 μg/ml); in addition, it showed stability in the presence of human serum for more than 24 h [86].
2.7 Histatins
Histatins belong to a distinct family of at least 12 low-molecular weight, histidine-rich cationic, salivary gland peptides with antimicrobial effect through the plasma membrane disruption [199]. Histatin-8, known as hemagglutination-inhibiting peptide [200], was the only member of this group that showed antimicrobial activity against A. baumannii, inhibiting the growth of both sensitive standard strains colistin-resistant mutant A. baumannii ATCC 19606 at 32 μg/ml [86].
2.8 Dermcidins
Dermcidin is an anionic AMP encoded by the DCD gene in humans essentially produced in eccrine sweat glands, secreted into a sweat, and further transported to the skin’s epidermal surface [130, 201]. It has two parts; N-terminal peptide promotes neural cell survival under severe oxidative stress conditions called DCD-1 L [130]. DCD-1 L, a C-terminal peptide with the net electric charge of −2, is the only anionic anti-Acinetobacter natural AMP found in the literature that shows partial helicity in solution [130, 182]. Interestingly, in exposure to this AMP, the PDR A. baumannii isolates are twice more susceptible as XDR isolates and the standard strain (ATCC 19606) (MIC = 8 μg/ ml) [131].
2.9 Tachyplesin III
Tachyplesin III, isolated from the hemolymph of the Southeast Asian horseshoe crabs Tachypleus gigas and Carcinoscorpius rotundicauda, consists of 17 amino acids with two disulfide bridges and is a representative antimicrobial peptide with a cyclic β-sheet structure. However, its potential toxicity hampers its use in mammalian cells [202]. Nevertheless, Tachyplesin III could inhibit the XDR A. baumannii strains (8–16 μg/ml) and at 2 × MIC, eliminating the XDR A. baumannii strains [203].
2.10 Computationally designed antimicrobial peptide
The biosynthesis of AMPs can be a starting point for obtaining AMPS with functions similar to natural ones, being an attractive therapeutic option for preventing and controlling infections. In this sense, bioinformatics and computer science have been widely used in various aspects in many studies of A. baumannii, such as design evaluation of AMPs [136, 204, 205, 206, 207, 208], which includes two general principles that increased antimicrobial activity and reduced toxicity against eukaryotic cells [209, 210]. As an example of synthetic AMPs, we have stapled AMP [137] and PNA (RXR) 4XB, an antisense nucleic acid peptide compound [138] with intense bactericidal activity. The synthetic RR is a small α-helical AMP with fast bactericidal activity capable of retaining the antimicrobial property at physiological concentrations of NaCl and MgCl2 [132]. The anti-A. baumannii effect of RR against sensitive and MDR strains inhibits the growth at 25–99 μg/ml concentration. Two new analogs of this peptide were introduced with much stronger anti-A. baumannii properties than RR, and the AMPs RR2 and RR4 inhibit the growth of sensitive and drug-resistant strains (3–6 μg/ml) [211]. The peptide DP7 inhibits the growth of antibiotic-resistant A. baumannii strains at 4–16 μg/ml concentration, and the synergistic effects were showed after simultaneous treatment of some drug-resistant A. baumannii isolates with DP7 and antibiotics such as amoxicillin, azithromycin, and vancomycin [133]. Zhang et al. showed that DP7 invades the microbial cell through various pathways after sequencing the transcriptome of the bacteria exposed to this peptide [134]. Omega76 is a cationic AMP with an α-helical structure, causing death in A. baumannii through membrane disruption. This peptide was designed based on the maximum common subgraph of helices and further introduced as an appropriate alternative for colistin due to its high anti-A. baumannii activity against carbapenem and tigecycline-resistant isolates (MBC = 2–8 μg/ml) and lack of toxicity in the mouse model [135].
3. Resistance to AMPS
Although AMPs have a low likelihood to select for resistance, similar to the conventional antibiotics, another challenge is represented by the numerous reports describing the development of resistance mechanisms against some AMPs, including proteolytic degradation or sequestration by secreted proteins, impedance by exopolymers, and biofilm matrix molecules, circumvention of attraction by cell surface/membrane alteration, and export by efflux pumps [212, 213, 214, 215, 216]. The development of resistance to colistin by A. baumannii following long-term clinical application was observed [217, 218]. In A. baumannii stable colistin resistance was also observed following direct plating with the complete loss of LPS production due to the inactivation of one of three genes involved in lipid A biosynthesis (lpxA, lpxD, or lpxC). Resistance to colistin is an important clinical issue, considering that colistin is a last-resort drug used to treat MDR nosocomial pathogens [218, 219, 220]. Several mechanisms have been reported responsible for resistance to AMPs, including expression of efflux pumps, increased secretion of proteolytic enzymes, and surface charge modification to avoid membrane-peptide electrostatic interactions [213, 221, 222].
For delivering the AMPs, several nanocarriers were developed, which may help avoid the low bioavailability, proteolysis, or susceptibility and toxicity associated with APMs [223, 224]. Changes in the molecular structure, modifications of biochemical characterization, and combination with common antibiotics have been reported to reduce AMP resistance [214]. The aprotinin is the first inhibitor identified to inhibit AMP resistance in multiple pathogens [225].
4. Conclusion(s)
A. baumannii is one of the ESKCAPE pathogens responsible for nosocomial and community-acquired infections, with the incidence of MDR and virulent clones increasingly worldwide. The enormous adaptability of A. baumannii, as well as the remarkable ability to acquire determinants of resistance, allied to your innate ability to form biofilms, contributes to the inefficiency of most current therapeutic strategies, determining the transition to the “post-antibiotic era” and highlighting the necessity to develop new therapeutic approaches. In this context, natural and synthetic AMPs emerge as potential next-generation antibiotics to mitigate a wide array of microbial infections, including those caused by MDR A. baumannii strains. Moreover, the antimicrobial activity of these peptides can be effectively increased by minor modifications through the development of computer science and bioinformatics. The synthetic AMPs present a promising solution to overcome the drawbacks of using natural AMPs. They contain critical features based on natural AMPs, with slight modifications to achieve higher antimicrobial efficiency and improved chemical stability. In this research, we observed the main properties of anti-A. baumannii peptides with some common characteristics, such as 1. The α-helical structure was predominant. 2. Most peptides have a positive charge, and in many cases, there is a direct relationship between an increased positive charge and your activity. 3. The action mechanisms of these peptides are direct membrane attack and intracellular targeting or both simultaneously. Unfortunately, considerable experimental data describe how bacteria can develop resistance to AMPs, such as colistin and polymyxin B in A. baumannii. Since AMPS are considered potential novel antimicrobial drugs, understanding the mechanism of bacterial resistance to direct killing of AMPS is of great significance.
Conflict of interest
The authors declare no conflict of interest.
Notes/thanks/other declarations
We thank D. Guilherme Curty Lechuga by the drawing of figures 1 and 2 of this chapter.
\n',keywords:"RAMP, Acinetobacter baumannii, resistance, action mechanism",chapterPDFUrl:"https://cdn.intechopen.com/pdfs/81299.pdf",chapterXML:"https://mts.intechopen.com/source/xml/81299.xml",downloadPdfUrl:"/chapter/pdf-download/81299",previewPdfUrl:"/chapter/pdf-preview/81299",totalDownloads:18,totalViews:0,totalCrossrefCites:0,dateSubmitted:"July 23rd 2021",dateReviewed:"September 9th 2021",datePrePublished:"April 16th 2022",datePublished:null,dateFinished:"April 16th 2022",readingETA:"0",abstract:"Antibiotic poly-resistance (multi drug-, extreme-, and pan-drug resistance) is a major global threat to public health. Unfortunately, in 2017, the World Health Organization (WHO) introduced the carbapenemresistant isolates in the priority pathogens list for which new effective antibiotics or new ways of treating the infections caused by them are urgently needed. Acinetobacter baumannii is one of the most critical ESKAPE pathogens for which the treatment of resistant isolates have caused severe problems; its clinically significant features include resistance to UV light, drying, disinfectants, and antibiotics. Among the various suggested options, one of the antimicrobial agents with high potential to produce new anti-Acinetobacter drugs is the antimicrobial peptides (AMPs). AMPs are naturally produced by living organisms and protect the host against pathogens as a part of innate immunity. The main mechanisms action of AMPs are the ability to cause cell membrane and cell wall damage, the inhibition of protein synthesis, nucleic acids, and the induction of apoptosis and necrosis. AMPs would be likely among the main anti-A. baumannii drugs in the post-antibiotic era. Also, the application of computer science to increase anti-A. baumannii activity and reduce toxicity is also being developed.",reviewType:"peer-reviewed",bibtexUrl:"/chapter/bibtex/81299",risUrl:"/chapter/ris/81299",signatures:"Karyne Rangel and Salvatore Giovanni De-Simone",book:{id:"10874",type:"book",title:"Antimicrobial Peptides",subtitle:null,fullTitle:"Antimicrobial Peptides",slug:null,publishedDate:null,bookSignature:"Dr. Shymaa Enany, Dr. Jorge Adrian Masso-Silva and Ph.D. Anna Savitskaya",coverURL:"https://cdn.intechopen.com/books/images_new/10874.jpg",licenceType:"CC BY 3.0",editedByType:null,isbn:"978-1-83969-714-2",printIsbn:"978-1-83969-713-5",pdfIsbn:"978-1-83969-715-9",isAvailableForWebshopOrdering:!0,editors:[{id:"81926",title:"Dr.",name:"Shymaa",middleName:null,surname:"Enany",slug:"shymaa-enany",fullName:"Shymaa Enany"}],productType:{id:"1",title:"Edited Volume",chapterContentType:"chapter",authoredCaption:"Edited by"}},authors:null,sections:[{id:"sec_1",title:"1. Introduction",level:"1"},{id:"sec_2",title:"2. Antimicrobial peptides",level:"1"},{id:"sec_2_2",title:"2.1 Cathelicidins",level:"2"},{id:"sec_2_3",title:"2.1.1 LL-37",level:"3"},{id:"sec_3_3",title:"2.1.2 Snake cathelicidins",level:"3"},{id:"sec_4_3",title:"2.1.3 Alligator cathelicidins",level:"3"},{id:"sec_5_3",title:"2.1.4 Wallaby antimicrobial",level:"3"},{id:"sec_6_3",title:"2.1.5 Bovine cathelicidins (Indolicidin and Bactenecin)",level:"3"},{id:"sec_8_2",title:"2.2 Defensins",level:"2"},{id:"sec_8_3",title:"2.2.1 α-Defensins (HNPs and HD5)",level:"3"},{id:"sec_9_3",title:"2.2.2 β-Defensins",level:"3"},{id:"sec_10_3",title:"2.2.3 α-Helical and antiparallel β-sheet defensins",level:"3"},{id:"sec_12_2",title:"2.3 Frog antimicrobial peptides",level:"2"},{id:"sec_12_3",title:"2.3.1 Magainin and pexiganan (its analog)",level:"3"},{id:"sec_13_3",title:"2.3.2 Brevinin-2 related peptide (B2RP)",level:"3"},{id:"sec_14_3",title:"2.3.3 B2RP-ERa",level:"3"},{id:"sec_15_3",title:"2.3.4 Alyteserins",level:"3"},{id:"sec_16_3",title:"2.3.5 Peptide glycine-leucine-amide",level:"3"},{id:"sec_17_3",title:"2.3.6 Caerulein precursor fragment (CPF)",level:"3"},{id:"sec_18_3",title:"2.3.7 Hymenochirins",level:"3"},{id:"sec_19_3",title:"2.3.8 XT-7",level:"3"},{id:"sec_20_3",title:"2.3.9 Buforins",level:"3"},{id:"sec_22_2",title:"2.4 Melittin",level:"2"},{id:"sec_23_2",title:"2.5 Cecropins",level:"2"},{id:"sec_24_2",title:"2.6 Mastoparan",level:"2"},{id:"sec_25_2",title:"2.7 Histatins",level:"2"},{id:"sec_26_2",title:"2.8 Dermcidins",level:"2"},{id:"sec_27_2",title:"2.9 Tachyplesin III",level:"2"},{id:"sec_28_2",title:"2.10 Computationally designed antimicrobial peptide",level:"2"},{id:"sec_30",title:"3. Resistance to AMPS",level:"1"},{id:"sec_31",title:"4. Conclusion(s)",level:"1"},{id:"sec_35",title:"Conflict of interest",level:"1"},{id:"sec_32",title:"Notes/thanks/other declarations",level:"1"}],chapterReferences:[{id:"B1",body:'O’Neill J. Tackling Drug-Resistance Infections Globally: Final Report and Recommendations. The Review on Antimicrobial Resistance. London, UK: Government of the United Kingdom; 2016. 84 p'},{id:"B2",body:'Tacconelli E, Carrara A, Savoldi S, Harbarth M, Mendelson DL, Monnet C, et al. Discovery, research, and development of new antibiotics: The WHO priority list of antibiotic-resistant bacteria and tuberculosis. The Lancet Infectious Diseases. 2018;18(3):318-327'},{id:"B3",body:'Lewis K. Persister cells, dormancy, and infectious disease. Nature Reviews. Microbiology. 2007;5(1):48-56'},{id:"B4",body:'Lewis K. Persister cells. Annual Review of Microbiology. 2010;64:357-372. 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Anticancer Research. 2002;22(5):2811-2816'},{id:"B193",body:'Wu Q, Patočka J, Kuča K. Insect Antimicrobial Peptides, a Mini Review. Toxins (Basel). 2018;10(11):461. DOI: 10.3390/toxins10110461'},{id:"B194",body:'Yun J, Lee DG. Cecropin A-induced apoptosis is regulated by ion balance and glutathione antioxidant system in Candida albicans. IUBMB Life. 2016;68(8):652-662. DOI: 10.1002/iub.1527'},{id:"B195",body:'Hirai Y, Yasuhara T, Yoshida H, Nakajima T, Fujino M, Kitada C. A new mast cell degranulating peptide “mastoparan” in the venom of Vespula lewisii. Chem Pharm Bull (Tokyo). 1979;27(8):1942-1944. DOI: 10.1248/cpb.27.1942'},{id:"B196",body:'Moreno M, Giralt E. Three valuable peptides from bee and wasp venoms for therapeutic and biotechnological use: Melittin apamin and mastoparan. Toxins. 2015;7(4):1126-1150. DOI: 10.3390/toxins7041126'},{id:"B197",body:'Chen X, Zhang L, Wu Y, Wang L, Ma C, Xi X, et al. 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FEMS Microbiology Letters. 1992;77(1–3):201-204. DOI: 10.1016/0378-1097(92)90156-i'},{id:"B201",body:'Burian M, Schittek B. The secrets of dermcidin action. International Journal of Medical Microbiology. 2015;305(2):283-286. DOI: 10.1016/j.ijmm.2014.12.012'},{id:"B202",body:'Muta T, Fujimoto T, Nakajima H, Iwanaga S. Tachyplesins isolated from hemocyte of southeast Asian horseshoe crabs (Carcinoscorpius rotundicauda and Tachypleus gigas): Identification of a new tachyplesin tachyplesin III and a processing intermediate of its precursor. Journal of Biochemistry. 1990;108(9):261-266. DOI: 10.1093/oxfordjournals. jbchem.a123191'},{id:"B203",body:'Liu C, Qi J, Shan B, Ma Y. Tachyplesin causes membrane instability that kills multidrug-resistant bacteria by inhibiting the 3-ketoacyl carrier protein reductase FabG. Frontiers in Microbiology. 2018;9:825. DOI: 10.3389/fmicb.2018.00825'},{id:"B204",body:'Rahbar MR, Zarei M, Jahangiri A, Khalili S, Nezafat N, Negahdaripour M, et al. Pierce into the native structure of Ata, a trimeric autotransporter of Acinetobacter baumannii ATCC 17978. Int. J. Pept. Res. Therapeut. 2020;26:1269-1282'},{id:"B205",body:'Jahangiri A, Rasooli I, Owlia P, Fooladi AAI, Salimian J. An integrative in silico approach to the structure of Omp33-36 in Acinetobacter baumannii. Computational Biology and Chemistry. 2018;72:77-86. DOI: 10.1016/j.compbiolchem.2018.01.003'},{id:"B206",body:'Rasooli I, Abdolhamidi R, Jahangiri A, Astaneh DAS. Outer membrane protein Oma87 prevents Acinetobacter baumannii infection. International Journal of Peptide Research and Therapeutics. 2020;9:1-8. DOI: 10.1007/s10989-020-10056-0'},{id:"B207",body:'Rahbar MR, Zarei M, Jahangiri A, Khalili S, Nezafat N, Negahdaripour M, et al. Trimeric autotransporter adhesins in Acinetobacter baumannii coincidental evolution at work. Infection, Genetics and Evolution. 2019;71:116-127. DOI: 10.1016/j. meegid.2019.03.023'},{id:"B208",body:'Nagarajan D, Nagarajan T, Roy N, Kulkarni O, Ravichandran S, Mishra M, et al. The Journal of Biological Chemistry. 2018;293(10):3492-3509. DOI: 10.1074/jbc.M117.805499'},{id:"B209",body:'Misawa T, Goto C, Shibata N, Hirano M, Kikuchi Y, Naito M, et al. Rational design of novel amphipathic antimicrobial peptides focused on the distribution of cationic amino acid residues. Med. Chem. Comm. 2019;10(6):896-900. DOI: 10.1039/c9md0 0166b'},{id:"B210",body:'Khan MTH. Recent Trends on QSAR in the Pharmaceutical Perceptions. Sharjah, United Arab Emirates: Bentham Science Publishers; 2012. ISBN: 978-1-60805-433-6'},{id:"B211",body:'Wu X, Wang Z, Li X, Fan Y, He G, Wan Y, et al. In vitro and in vivo activities of antimicrobial peptides developed using an amino acid-based activity prediction method. Antimicrobial Agents and Chemotherapy. 2014;58(9):5342-5349'},{id:"B212",body:'Ageitos JM, Sánchez-Pérez A, Calo-Mata P, Villa TG. Antimicrobial peptides (AMPs): Ancient compounds that represent novel weapons in the fight against bacteria. Biochemical Pharmacology. 2017;133:117. DOI: 10.1016/j.bcp.2016.09.018'},{id:"B213",body:'Andersson DI, Hughes D, Kubicek-Sutherland JZ. Mechanisms and consequences of bacterial resistance to antimicrobial peptides. Drug Resistance Updates. 2016;26:43-57. DOI: 10.1016/j.drup. 2016.04.002'},{id:"B214",body:'Moravej H, Moravej Z, Yazdanparast M, Heiat M, Mirhosseini A, Moghaddam MM, et al. Antimicrobial peptides: Features action and their resistance mechanisms in bacteria. Microbial Drug Resistance. 2018;24(6):747. DOI: 10.1089/mdr.2017.0392'},{id:"B215",body:'Joo HS, Fu CI, Otto M. Bacterial strategies of resistance to antimicrobial peptides. Phil. Trans. R. Soc. Lond. B. Biol. Sci. 2016;371(1695):20150292. DOI: 10.1098/rstb. 2015.0292'},{id:"B216",body:'Omardien S, Brul S, Zaat SAJ. Antimicrobial activity of cationic antimicrobial peptides against gram-positive: Current progress made in understanding the mode of action and the response of bacteria. Front. Cell. Develop. Biol. 2016;4:111. DOI: 10.3389/fcell.2016.00111'},{id:"B217",body:'Jeannot K, Bolard A, Plésiat P. Resistance to polymyxins in gram-negative organisms. Int. J. Antimicr Ag. 2017;49(5):526-535. DOI: 10.1016/j.ijantimicag.2016. 11.029'},{id:"B218",body:'Liu YY, Wang Y, Walsh TR, Yi LX, Zhang R, Spencer J, et al. Emergence of plasmid-mediated colistin resistance mechanism MCR-1 in animals and human beings in China: A microbiological and molecular biological study. The Lancet Infectious Diseases. 2016;16(2):161-168. DOI: 10.1016/S1473-3099(15)00424-7'},{id:"B219",body:'Paterson DL, Harris PNA. Colistin resistance: A major breach in our last line of defense. The Lancet Infectious Diseases. 2016;16(2):132-133. 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Cost-effective downstream processing of recombinantly produced pexiganan peptide and its antimicrobial activity. AMB Express. 2018;8(1):1-14. DOI: 10.1186/s13568-018-0541-3'},{id:"B225",body:'Brannon JR, Burk DL, Leclerc JM, Thomassin JL, Portt A, Berghuis AM, et al. Inhibition of outer membrane proteases of the omptin family by aprotinin. Infection and Immunity. 2015;83(6):2300-2311. DOI: 10.1128/IAI.00136-15'}],footnotes:[],contributors:[{corresp:null,contributorFullName:"Karyne Rangel",address:null,affiliation:'
Center for Technological Development in Health (CDTS)/National Institute of Science and Technology for Innovation in Neglected Diseases Populations (INCT-IDPN), FIOCRUZ, Brazil
'},{corresp:"yes",contributorFullName:"Salvatore Giovanni De-Simone",address:"dsimone@cdts.fiocruz.br",affiliation:'
Center for Technological Development in Health (CDTS)/National Institute of Science and Technology for Innovation in Neglected Diseases Populations (INCT-IDPN), FIOCRUZ, Brazil
Epidemiology and Molecular Systematics Laboratory, Oswaldo Cruz Institute, FIOCRUZ, Brazil
Biology Institute, Molecular and Cellular Biology, Department, Federal Fluminense University, Brazil
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Among the mammal species inhabiting tropical forests along Ecuador’s coast, wild cats such as ocelots (Leopardus pardalis), jaguarundis (Puma yagouaroundi), cougars (Puma concolor) and jaguars (Panthera onca) are a key group of carnivores deserving critical consideration because these species are facing several anthropogenic threats and conservation challenges. Of particularly attention is the critically endangered subspecies of jaguar (Panthera onca centralis) from the Ecuadorian coast. Despite this species is the largest cat in Ecuador’s coastal tropical forests and demanding large territories to survive, little is known about its population and conservation status. In most forests along Ecuador’s coast, habitat loss due to deforestation and fragmentation, poaching of prey and illegal hunting threaten the survival of jaguars and questions linger about its ecology and population health. Based on recent field observations using transects and deployment of camera traps, as well as surveys conducted with the local community in and around Cerro Blanco Protected Forest and surrounding areas of the Cordillera Chongón-Colonche Mountain Range, we advance the state of the ecological knowledge of coastal jaguar populations with conservation implications of its threatened habitat and long-term survival in Ecuador.",signatures:"Miguel Saavedra Mendoza, Paúl Cun, Eric Horstman, Sonia\nCarabajo and Juan José Alava",authors:[{id:"53467",title:"Dr.",name:"Juan Jose",surname:"Alava",fullName:"Juan Jose Alava",slug:"juan-jose-alava",email:"jalavasa@sfu.ca"},{id:"203749",title:"Mr.",name:"Miguel",surname:"Saavedra Mendoza",fullName:"Miguel Saavedra Mendoza",slug:"miguel-saavedra-mendoza",email:"miguel_saavedra80@hotmail.com"},{id:"203750",title:"M.Sc.",name:"Paul",surname:"Cun",fullName:"Paul Cun",slug:"paul-cun",email:"epcl1978@hotmail.com"},{id:"203751",title:"MSc.",name:"Eric",surname:"Horstman",fullName:"Eric Horstman",slug:"eric-horstman",email:"horstman.eric2@gmail.com"},{id:"203752",title:"MSc.",name:"Sonia",surname:"Carabajo",fullName:"Sonia Carabajo",slug:"sonia-carabajo",email:"soncarabajo@gmail.com"}],book:{id:"5993",title:"Big Cats",slug:"big-cats",productType:{id:"1",title:"Edited Volume"}}}],collaborators:[{id:"53467",title:"Dr.",name:"Juan Jose",surname:"Alava",slug:"juan-jose-alava",fullName:"Juan Jose Alava",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/53467/images/1675_n.jpg",biography:"Juan Jose Alava is a Biologist who graduated from the Universidad de Guayaquil, Ecuador, in 1996. In the 1990s, during his undergraduate studies, he got deeply involved with research and conservation of marine mammals, Neotropical birds, and sea turtles as well as the identification of tropical parasites. During the mid-1990s, he started working as a Microbiology Research Assistant at the National Institute of Hygiene and Tropical Medicine of Ecuador and as a Wildlife Biologist specialized in environmental impact assessments at the Center of Environmental Studies (CEMA, Centro de Estudios de Medio Ambiente de la ESPOL, Guayaquil, Ecuador) for several years (1995–2002). He was also an instructor of zoology and ecological projects at the undergraduate level at the Escuela de Ecoturismo, Universidad Cristiana Latino Americana, Ecuador. He received his Master degree (Master of Earth and Environmental Resource Management), under a Fulbright Scholarship, from the School of Ocean, Earth, and Environment, College of Art and Sciences, University of South Carolina,Columbia USA. He received the Ph.D. degree (specialized in environmental toxicology and environmental resource management) from the School of Resource and Environmental Management (REM School), Faculty of Environment, Simon Fraser University (SFU), British Columbia, Canada, in 2011. His Ph.D. dissertation was focused on ecotoxicology regarding the baseline levels, biomagnification, and health effects of persistent organic pollutants (POPs) in endangered Galapagos sea lion pups of the Galapagos Islands and food web bioaccumulation modeling in threatened marine mammals (killer whales, Steller sea lions) from British Columbia. He has served as an instructor for Population Dynamics, Global Changes, Applied Ecology and Sustainable Environments, and Chemical Pesticides and the Environment at SFU. He is also an Associate Faculty Member at Royal Roads University (Victoria, BC, Canada), where he was an instructor for Environmental Chemistry. 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A dynamic career research platform which is based on the thematic areas of comparative vertebrate physiology, stress endocrinology, reproductive endocrinology, animal health and welfare, and conservation biology. \nEdward has supervised 40 research students and published over 60 peer reviewed research.",institutionString:null,institution:{name:"University of Queensland",institutionURL:null,country:{name:"Australia"}}},{id:"265070",title:"Dr.",name:"Hussein Abdelhay",surname:"Essayed Kaoud",slug:"hussein-abdelhay-essayed-kaoud",fullName:"Hussein Abdelhay Essayed Kaoud",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/265070/images/system/265070.png",biography:"Dr. Hussein Kaoud was the Chairman of the Department of Preventive Medicine at Cairo University. He has given lectures in Molecular Epidemiology and Biotechnology at different universities and has been a member of many International Publishing Houses, Reviewer, and Editor for indexed journals. Currently, he works as Full Professor of Preventive Medicine at Cairo University, Egypt. His research interest is focused on Molecular Biology and Advanced Technology of Basic Life Sciences after he had his Ph.D. and D.Sc. He has published more than 300 publications. Dr. Hussein Kaoud has several international books, one international award (USA), 10 Cairo university International Publication awards and the Appreciation Award in Advanced Technological Sciences, from Cairo University. He supervised, examined and discussed many medical dissertations.",institutionString:"Cairo University",institution:{name:"Cairo University",institutionURL:null,country:{name:"Egypt"}}}]},generic:{page:{slug:"OA-publishing-fees",title:"Open Access Publishing Fees",intro:"
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An online manuscript tracking system to facilitate your work
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English language copyediting and proofreading, including the correction of grammatical, spelling, and other common errors
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XML Typesetting and pagination - web (PDF, HTML) and print files preparation
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Discoverability - electronic citation and linking via DOI
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Permanent and unrestricted online access to your work
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What isn't covered by the Open Access Publishing Fee?
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If your manuscript:
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Exceeds the number of pages defined by the publishing guidelines, an additional fee per page may be required
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If a manuscript requires Heavy Editing or Language Polishing, this will incur additional fees.
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Your Author Service Manager will inform you of any items not covered by the OAPF and provide exact information regarding those additional costs before proceeding.
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Open Access Funding
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To explore funding opportunities and learn more about how you can finance your IntechOpen publication, go to our Open Access Funding page. IntechOpen offers expert assistance to all of its Authors. We can support you in approaching funding bodies and institutions in relation to publishing fees by providing information about compliance with the Open Access policies of your funder or institution. We can also assist with communicating the benefits of Open Access in order to support and strengthen your funding request and provide personal guidance through your application process. You can contact us at funders@intechopen.com for further details or assistance.
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For Authors who are still unable to obtain funding from their institutions or research funding bodies for individual projects, IntechOpen does offer the possibility of applying for a Waiver to offset some or all processing feed. Details regarding our Waiver Policy can be found here.
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Added Value of Publishing with IntechOpen
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Choosing to publish with IntechOpen ensures the following benefits:
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Indexing and listing across major repositories, see details ...
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Long-term archiving
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Visibility on the world's strongest OA platform
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Live Performance Metrics to track readership and the impact of your chapter
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Dissemination and Promotion
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Benefits of Publishing with IntechOpen
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Proven world leader in Open Access book publishing with over 10 years experience
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Most competitive prices in the market
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Optimized processes that assure your research is made available to the scientific community without delay
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Personal support during every step of the publication process
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+184,650 citations in Web of Science databases
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Currently strongest OA platform with over 175 million downloads
As a gold Open Access publisher, an Open Access Publishing Fee is payable on acceptance following peer review of the manuscript. In return, we provide high quality publishing services and exclusive benefits for all contributors. IntechOpen is the trusted publishing partner of over 140,000 international scientists and researchers.
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The Open Access Publishing Fee (OAPF) is payable only after your book chapter, monograph or journal article is accepted for publication.
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OAPF Publishing Options
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1,400 GBP Chapter - Edited Volume
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850 GBP Chapter - Book Series Topic (Annual Volume)
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10,000 GBP Monograph - Long Form
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4,000 GBP Compacts Monograph - Short Form
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850 GBP Journal Article (Across Portfolio)
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During the launching phase journals do not charge an APC, rather they will be funded by IntechOpen.
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*These prices do not include Value-Added Tax (VAT). Residents of European Union countries need to add VAT based on the specific rate in their country of residence. Institutions and companies registered as VAT taxable entities in their own EU member state will not pay VAT as long as provision of the VAT registration number is made during the application process. This is made possible by the EU reverse charge method.
\n\n
Services included are:
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An online manuscript tracking system to facilitate your work
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Personal contact and support throughout the publishing process from your dedicated Author Service Manager
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Assurance that your manuscript meets the highest publishing standards
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English language copyediting and proofreading, including the correction of grammatical, spelling, and other common errors
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XML Typesetting and pagination - web (PDF, HTML) and print files preparation
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Discoverability - electronic citation and linking via DOI
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Permanent and unrestricted online access to your work
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What isn't covered by the Open Access Publishing Fee?
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If your manuscript:
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Exceeds the number of pages defined by the publishing guidelines, an additional fee per page may be required
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If a manuscript requires Heavy Editing or Language Polishing, this will incur additional fees.
\n
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Your Author Service Manager will inform you of any items not covered by the OAPF and provide exact information regarding those additional costs before proceeding.
\n\n
Open Access Funding
\n\n
To explore funding opportunities and learn more about how you can finance your IntechOpen publication, go to our Open Access Funding page. IntechOpen offers expert assistance to all of its Authors. We can support you in approaching funding bodies and institutions in relation to publishing fees by providing information about compliance with the Open Access policies of your funder or institution. We can also assist with communicating the benefits of Open Access in order to support and strengthen your funding request and provide personal guidance through your application process. You can contact us at funders@intechopen.com for further details or assistance.
\n\n
For Authors who are still unable to obtain funding from their institutions or research funding bodies for individual projects, IntechOpen does offer the possibility of applying for a Waiver to offset some or all processing feed. Details regarding our Waiver Policy can be found here.
\n\n
Added Value of Publishing with IntechOpen
\n\n
Choosing to publish with IntechOpen ensures the following benefits:
\n\n
\n\t
Indexing and listing across major repositories, see details ...
\n\t
Long-term archiving
\n\t
Visibility on the world's strongest OA platform
\n\t
Live Performance Metrics to track readership and the impact of your chapter
\n\t
Dissemination and Promotion
\n
\n\n
Benefits of Publishing with IntechOpen
\n\n
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Proven world leader in Open Access book publishing with over 10 years experience
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+5,700 OA books published
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Most competitive prices in the market
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Fully compliant with OA funding requirements
\n\t
Optimized processes that assure your research is made available to the scientific community without delay
\n\t
Personal support during every step of the publication process
\n\t
+184,650 citations in Web of Science databases
\n\t
Currently strongest OA platform with over 175 million downloads
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Leaching is the vertical downward displacement of pesticides through the soil profile and the unsaturated zone, and finally to groundwater, which is vulnerable to pollution. Pesticides are frequently leached through the soil by the effect of rain or irrigation water. Pesticide leaching is highest for weakly sorbing and/or persistent compounds, climates with high precipitation and low temperatures, and soils with low organic matter and sandy texture. On the contrary, for pesticides with a low persistence that disappear quickly, the risk of groundwater pollution considerably decreases. Different and varied factors such as physical-chemical properties of the pesticide, a permeability of the soil, texture and organic matter content of the soil, volatilization, crop-root uptake, and method and dose of pesticide application are responsible for the leaching rate of the pesticides. Soils that are high in clays and organic matter will slow the movement of water, attach easily to many pesticides, and generally have a higher diversity and population of soil organisms that can metabolize the pesticides.",book:{id:"8533",slug:"pesticides-use-and-misuse-and-their-impact-in-the-environment",title:"Pesticides",fullTitle:"Pesticides - Use and Misuse and Their Impact in the Environment"},signatures:"Gabriel Pérez-Lucas, Nuria Vela, Abderrazak El Aatik and Simón Navarro",authors:[{id:"202983",title:"Dr.",name:"Simón",middleName:null,surname:"Navarro",slug:"simon-navarro",fullName:"Simón Navarro"},{id:"202988",title:"Dr.",name:"Nuria",middleName:null,surname:"Vela",slug:"nuria-vela",fullName:"Nuria Vela"},{id:"206059",title:"Dr.",name:"Gabriel",middleName:null,surname:"Pérez-Lucas",slug:"gabriel-perez-lucas",fullName:"Gabriel Pérez-Lucas"},{id:"283154",title:"Mr.",name:"Abderrazak",middleName:null,surname:"El Aatik",slug:"abderrazak-el-aatik",fullName:"Abderrazak El Aatik"}]},{id:"48594",doi:"10.5772/60911",title:"Environmental Exposure and Health Effects Associated with Malathion Toxicity",slug:"environmental-exposure-and-health-effects-associated-with-malathion-toxicity",totalDownloads:2668,totalCrossrefCites:15,totalDimensionsCites:31,abstract:"Malathion (O,O-dimethyl-S-1,2-bis ethoxy carbonyl ethyl phosphorodithionate) is a non-systemic, wide-spectrum pesticide. It is widely used throughout the world for agricultural, residential, and public health purposes, mainly to enhance food production and to provide protection from disease vectors. Malathion preference over other organophosphate pesticides relates to its low persistence in the environment as it is highly susceptible to hydrolysis, photolysis, and biodegradation. However, numerous malathion poisoning incidents including acute and chronic cases have been reported among pesticide workers and small children through accidental exposure. Malathion toxicity is compounded by its reactive metabolites and also depends upon the product purity, route of exposure, nutritional status, and gender of exposed individuals. Its metabolic oxidation in mammals, insects, and plants leads to the formation of malaoxon which appears to be several times more acutely toxic and represents the primary cause of malathion’s toxicity. Depending on the level of exposure, several signs and symptoms of toxicity including numbness, tingling sensation, headache, dizziness, difficulty breathing, weakness, irritation of skin, exacerbation of asthma, abdominal cramps, and death have been reported. Similar to other organophosphate pesticides, malathion exerts it toxic action by binding to acetylcholinesterase enzyme and inhibiting its activity, leading to accumulation of acetylcholine in synaptic junctions, which in turn results in overstimulation of cholinergic, muscarinic, and nicotinic receptors, and subsequent induction of adverse biologic effects. This chapter provides an update and analysis of the production and use, environmental occurrence, molecular mechanisms of toxicity, genotoxicity and carcinogenicity, and adverse human health effects associated with malathion exposure.",book:{id:"4637",slug:"toxicity-and-hazard-of-agrochemicals",title:"Toxicity and Hazard of Agrochemicals",fullTitle:"Toxicity and Hazard of Agrochemicals"},signatures:"Paul B. Tchounwou, Anita K. Patlolla, Clement G. Yedjou and\nPamela D. Moore",authors:[{id:"113353",title:"Prof.",name:"Paul",middleName:null,surname:"Tchounwou",slug:"paul-tchounwou",fullName:"Paul Tchounwou"}]},{id:"48553",doi:"10.5772/60767",title:"Ecotoxicology of Glyphosate and Glyphosate-Based Herbicides — Toxicity to Wildlife and Humans",slug:"ecotoxicology-of-glyphosate-and-glyphosate-based-herbicides-toxicity-to-wildlife-and-humans",totalDownloads:2576,totalCrossrefCites:10,totalDimensionsCites:19,abstract:"The use of agrochemicals, especially herbicides, is necessary to control pests in order to produce adequate food for the global population (estimated at 7 billion). Glyphosate and glyphosate-based herbicides have been used extensively for this purpose but recent studies have reported these chemical substances to be found in aquatic ecosystems, wildlife and humans in various quantities. In this chapter, we reviewed the impacts of glyphosate and glyphosate-based herbicides on wildlife and humans using measured endpoint effects caused by genotoxicity, cytotoxicity and reproductive toxicity. We used findings from different current investigations to demonstrate adverse effects, or otherwise, of glyphosate exposure to wildlife and humans. Our review reveals that glyphosate and its formulations may not only be considered as having genotoxic, cytotoxic or endocrine disrupting properties but they may also be causative agents of reproduction abnormalities in both wildlife and humans. Furthermore, the extensive use of glyphosate-based herbicides in genetically modified glyphosate-resistant plants grown for food and feed should be of grave concern since they can be sources of genotoxicity, cytotoxicity, and reproductive toxicity in wildlife and humans.",book:{id:"4637",slug:"toxicity-and-hazard-of-agrochemicals",title:"Toxicity and Hazard of Agrochemicals",fullTitle:"Toxicity and Hazard of Agrochemicals"},signatures:"Paul K. Mensah, Carolyn G. Palmer and Oghenekaro N. Odume",authors:[{id:"169135",title:"Dr.",name:"Paul",middleName:null,surname:"Mensah",slug:"paul-mensah",fullName:"Paul Mensah"},{id:"173888",title:"Prof.",name:"Carolyn",middleName:null,surname:"Palmer",slug:"carolyn-palmer",fullName:"Carolyn Palmer"},{id:"175580",title:"Dr.",name:"Oghenekaro Nelson",middleName:null,surname:"Odume",slug:"oghenekaro-nelson-odume",fullName:"Oghenekaro Nelson Odume"}]},{id:"65766",doi:"10.5772/intechopen.84161",title:"Pesticides, Anthropogenic Activities, and the Health of Our Environment Safety",slug:"pesticides-anthropogenic-activities-and-the-health-of-our-environment-safety",totalDownloads:1434,totalCrossrefCites:7,totalDimensionsCites:16,abstract:"Mankind depends on agricultural products for food consumption. Increasing population (more than 7 billion) requires significant growth in crop yield to meet essential demand. This aim was achieved through the use of pesticides to protect crops from diseases. Pesticides are toxic by design for organisms that can threaten food products. Their mode of action is by targeting systems or enzymes in the pests that may be similar to human system and therefore pose risks to human health and the environment as well. The WHO recommended classifying pesticides according to their toxicity and chemicals according to their chronic health and environmental hazards.",book:{id:"8533",slug:"pesticides-use-and-misuse-and-their-impact-in-the-environment",title:"Pesticides",fullTitle:"Pesticides - Use and Misuse and Their Impact in the Environment"},signatures:"Mona Saud AL-Ahmadi",authors:[{id:"276726",title:"Ph.D.",name:"Mona",middleName:null,surname:"AL-Ahmadi",slug:"mona-al-ahmadi",fullName:"Mona AL-Ahmadi"}]},{id:"48545",doi:"10.5772/60739",title:"Environmental Risk Assessment of Agrochemicals — A Critical Appraisal of Current Approaches",slug:"environmental-risk-assessment-of-agrochemicals-a-critical-appraisal-of-current-approaches",totalDownloads:2527,totalCrossrefCites:9,totalDimensionsCites:13,abstract:"This chapter provides insights into the difficulties and challenges of performing risk evaluations of agrochemicals. It is a critical review of the current methodologies used in ecological risk assessment of these chemicals, not their risks to humans. After an introduction to the topic, the current framework for ecological risk assessment is outlined. Two types of assessments are typically carried out depending on the purpose: i) regulatory assessments for registration of a chemical product; and ii) ecological assessments, for the protection of both terrestrial and aquatic ecosystems, which are usually site-specific. Although the general framework is well established, the methodologies used in each of the steps of the assessment are fraught with a number of shortcomings. Notwithstanding the subjectivity implicit in the evaluation of risks, there is scepticism in scientific circles about the appropriateness of the current methodologies because, after so many years of evaluations, we are still incapable of foreseeing the negative consequences that some agrochemicals have in the environment. A critical appraisal of such methodologies is imperative if we are to improve the current assessment process and fix the problems we face today. The chapter reviews first the toxicity assessment methods, pointing to the gaps in knowledge about this essential part of the process and suggesting avenues for further improvement. Deficiencies in the current regulations regarding toxicity testing are discussed, in particular the effect of the time factor on toxicity and the issue of complex mixtures. Other matters of concern are the extrapolation of toxicity data from the individual to the population and community levels, and the sub-lethal effects. The exposure assessment methods are dealt with in a second place. These rely on modelling and actual measurements of chemical residues in the environment. Various techniques employed to determine to exposure and bioavailability of agrochemicals to the various organisms in both aquatic and terrestrial ecosystems are reviewed. Again, the shortcomings and gaps in knowledge are addressed and suggestions for improvement are pointed out. Then, the process of putting together the information from the toxicity and exposure assessments to evaluate risks is discussed. Tiers I and II of the risk assessment are reviewed. The challenge here is to keep objectivity in the evaluations; this may require the introduction of new methods of risk assessment. Finally, the risk assessment implies establishing a management strategy that aims at reducing or minimising the impacts of agrochemicals under normal agricultural scenarios. Recommendations are often case-specific and need to be based on sound science as well as common sense principles. The chapter concludes with a summary of issues that need to be considered for improving risk assessments of agrochemicals.",book:{id:"4637",slug:"toxicity-and-hazard-of-agrochemicals",title:"Toxicity and Hazard of Agrochemicals",fullTitle:"Toxicity and Hazard of Agrochemicals"},signatures:"Francisco Sánchez-Bayo and Henk A. Tennekes",authors:[{id:"74970",title:"Dr.",name:"Francisco",middleName:null,surname:"Sánchez-Bayo",slug:"francisco-sanchez-bayo",fullName:"Francisco Sánchez-Bayo"},{id:"173845",title:"Dr.",name:"Henk",middleName:null,surname:"Tennekes",slug:"henk-tennekes",fullName:"Henk Tennekes"}]}],mostDownloadedChaptersLast30Days:[{id:"78542",title:"Mitigation of Climate Change by Nitrogen Managements in Agriculture",slug:"mitigation-of-climate-change-by-nitrogen-managements-in-agriculture",totalDownloads:274,totalCrossrefCites:1,totalDimensionsCites:1,abstract:"Soil is one of the important sources of nitrous oxide (N2O), which is generally producing through soil microbial processes, such as nitrification and denitrification. Agricultural soils receive chemical and organic fertilizers to maintain or increase crop yield and soil fertility, but several factors are influencing N2O emissions, such as types and conditions of soil and fertilizer, and rate, form, and timing of application. Mitigation of N2O is a challenging topic for future earth by using inhibitors, controlled-release fertilizers, and other amendments, but the cost and side effects should be considered for feasibility.",book:{id:"10360",slug:"nitrogen-in-agriculture-physiological-agricultural-and-ecological-aspects",title:"Nitrogen in Agriculture",fullTitle:"Nitrogen in Agriculture - Physiological, Agricultural and Ecological Aspects"},signatures:"Kazuyuki Inubushi and Miwa Yashima",authors:[{id:"108366",title:"Dr.",name:"Kazuyuki",middleName:null,surname:"Inubushi",slug:"kazuyuki-inubushi",fullName:"Kazuyuki Inubushi"},{id:"429712",title:"Dr.",name:"Miwa",middleName:null,surname:"Yashima",slug:"miwa-yashima",fullName:"Miwa Yashima"}]},{id:"48594",title:"Environmental Exposure and Health Effects Associated with Malathion Toxicity",slug:"environmental-exposure-and-health-effects-associated-with-malathion-toxicity",totalDownloads:2672,totalCrossrefCites:16,totalDimensionsCites:31,abstract:"Malathion (O,O-dimethyl-S-1,2-bis ethoxy carbonyl ethyl phosphorodithionate) is a non-systemic, wide-spectrum pesticide. It is widely used throughout the world for agricultural, residential, and public health purposes, mainly to enhance food production and to provide protection from disease vectors. Malathion preference over other organophosphate pesticides relates to its low persistence in the environment as it is highly susceptible to hydrolysis, photolysis, and biodegradation. However, numerous malathion poisoning incidents including acute and chronic cases have been reported among pesticide workers and small children through accidental exposure. Malathion toxicity is compounded by its reactive metabolites and also depends upon the product purity, route of exposure, nutritional status, and gender of exposed individuals. Its metabolic oxidation in mammals, insects, and plants leads to the formation of malaoxon which appears to be several times more acutely toxic and represents the primary cause of malathion’s toxicity. Depending on the level of exposure, several signs and symptoms of toxicity including numbness, tingling sensation, headache, dizziness, difficulty breathing, weakness, irritation of skin, exacerbation of asthma, abdominal cramps, and death have been reported. Similar to other organophosphate pesticides, malathion exerts it toxic action by binding to acetylcholinesterase enzyme and inhibiting its activity, leading to accumulation of acetylcholine in synaptic junctions, which in turn results in overstimulation of cholinergic, muscarinic, and nicotinic receptors, and subsequent induction of adverse biologic effects. This chapter provides an update and analysis of the production and use, environmental occurrence, molecular mechanisms of toxicity, genotoxicity and carcinogenicity, and adverse human health effects associated with malathion exposure.",book:{id:"4637",slug:"toxicity-and-hazard-of-agrochemicals",title:"Toxicity and Hazard of Agrochemicals",fullTitle:"Toxicity and Hazard of Agrochemicals"},signatures:"Paul B. Tchounwou, Anita K. Patlolla, Clement G. Yedjou and\nPamela D. Moore",authors:[{id:"113353",title:"Prof.",name:"Paul",middleName:null,surname:"Tchounwou",slug:"paul-tchounwou",fullName:"Paul Tchounwou"}]},{id:"64602",title:"Environmental Risk of Groundwater Pollution by Pesticide Leaching through the Soil Profile",slug:"environmental-risk-of-groundwater-pollution-by-pesticide-leaching-through-the-soil-profile",totalDownloads:3016,totalCrossrefCites:21,totalDimensionsCites:60,abstract:"Adsorption, degradation, and movement are the key processes conditioning the behavior and fate of pesticides in the soil. Six processes that can move pesticides are leaching, diffusion, volatilization, erosion and run-off, assimilation by microorganisms, and plant uptake. Leaching is the vertical downward displacement of pesticides through the soil profile and the unsaturated zone, and finally to groundwater, which is vulnerable to pollution. Pesticides are frequently leached through the soil by the effect of rain or irrigation water. Pesticide leaching is highest for weakly sorbing and/or persistent compounds, climates with high precipitation and low temperatures, and soils with low organic matter and sandy texture. On the contrary, for pesticides with a low persistence that disappear quickly, the risk of groundwater pollution considerably decreases. Different and varied factors such as physical-chemical properties of the pesticide, a permeability of the soil, texture and organic matter content of the soil, volatilization, crop-root uptake, and method and dose of pesticide application are responsible for the leaching rate of the pesticides. Soils that are high in clays and organic matter will slow the movement of water, attach easily to many pesticides, and generally have a higher diversity and population of soil organisms that can metabolize the pesticides.",book:{id:"8533",slug:"pesticides-use-and-misuse-and-their-impact-in-the-environment",title:"Pesticides",fullTitle:"Pesticides - Use and Misuse and Their Impact in the Environment"},signatures:"Gabriel Pérez-Lucas, Nuria Vela, Abderrazak El Aatik and Simón Navarro",authors:[{id:"202983",title:"Dr.",name:"Simón",middleName:null,surname:"Navarro",slug:"simon-navarro",fullName:"Simón Navarro"},{id:"202988",title:"Dr.",name:"Nuria",middleName:null,surname:"Vela",slug:"nuria-vela",fullName:"Nuria Vela"},{id:"206059",title:"Dr.",name:"Gabriel",middleName:null,surname:"Pérez-Lucas",slug:"gabriel-perez-lucas",fullName:"Gabriel Pérez-Lucas"},{id:"283154",title:"Mr.",name:"Abderrazak",middleName:null,surname:"El Aatik",slug:"abderrazak-el-aatik",fullName:"Abderrazak El Aatik"}]},{id:"77770",title:"Mycorrhizal Fungi and Sustainable Agriculture",slug:"mycorrhizal-fungi-and-sustainable-agriculture",totalDownloads:284,totalCrossrefCites:0,totalDimensionsCites:1,abstract:"The 20thcentury witnessed an augmentation in agricultural production, mainly through the progress and use of pesticides, fertilizers containing nitrogen and phosphorus, and developments in plant breeding and genetic skills. In the naturally existing ecology, rhizospheric soils have innumerable biological living beings to favor the plant development, nutrient assimilation, stress tolerance, disease deterrence, carbon seizing and others. These organisms include mycorrhizal fungi, bacteria, actinomycetes, etc. which solubilize nutrients and assist the plants in up taking by roots. Amongst them, arbuscular mycorrhizal (AM) fungi have key importance in natural ecosystem, but high rate of chemical fertilizer in agricultural fields is diminishing its importance. The majority of the terrestrial plants form association with Vesicular Arbuscular Mycorrhiza (VAM) or Arbuscular Mycorrhizal fungi (AMF). This symbiosis confers benefits directly to the host plant’s growth and development through the acquisition of Phosphorus (P) and other mineral nutrients from the soil by the AMF. They may also enhance the protection of plants against pathogens and increases the plant diversity. This is achieved by the growth of AMF mycelium within the host root (intra radical) and out into the soil (extra radical) beyond. Proper management of Arbuscular Mycorrhizal fungi has the potential to improve the profitability and sustainability of agricultural systems. AM fungi are especially important for sustainable farming systems because AM fungi are efficient when nutrient availability is low and when nutrients are bound to organic matter and soil particles.",book:{id:"10360",slug:"nitrogen-in-agriculture-physiological-agricultural-and-ecological-aspects",title:"Nitrogen in Agriculture",fullTitle:"Nitrogen in Agriculture - Physiological, Agricultural and Ecological Aspects"},signatures:"Soibam Helena Devi, Ingudam Bhupenchandra, Soibam Sinyorita, S.K. Chongtham and E. Lamalakshmi Devi",authors:[{id:"301167",title:"Dr.",name:"E. Lamalakshmi",middleName:null,surname:"Devi",slug:"e.-lamalakshmi-devi",fullName:"E. Lamalakshmi Devi"},{id:"311911",title:"Dr.",name:"S.K.",middleName:null,surname:"Chongtham",slug:"s.k.-chongtham",fullName:"S.K. Chongtham"},{id:"345840",title:"Dr.",name:"Ingudam",middleName:null,surname:"Bhupenchandra",slug:"ingudam-bhupenchandra",fullName:"Ingudam Bhupenchandra"},{id:"423173",title:"Mrs.",name:"Soibam",middleName:null,surname:"Helena Devi",slug:"soibam-helena-devi",fullName:"Soibam Helena Devi"},{id:"423177",title:"Dr.",name:"Soibam",middleName:null,surname:"Sinyorita",slug:"soibam-sinyorita",fullName:"Soibam Sinyorita"}]},{id:"77147",title:"Influence of Heavy Metals on the Nitrogen Metabolism in Plants",slug:"influence-of-heavy-metals-on-the-nitrogen-metabolism-in-plants",totalDownloads:263,totalCrossrefCites:0,totalDimensionsCites:1,abstract:"As an essential element, Nitrogen is needed in large quantities for being an important component of cellular constituents and for plant metabolism, and its deficiency is one of the most common limitations for plant development. The study of the toxic effects of metal in plants involves a complex system of reactions that can be better determined once having a large attention of the different backgrounds of occurence to determinate how to proceed. The objective of this review is to add scientific knowledge, addressing the main functionalities and characteristics of this relation heavy metals – nitrogen metabolism in plant. Increasing industrialization and urbanization had anthropogenic contribution of heavy metals in biosphere and had largest availability in ecosystems. This toxicity in plants varies with plant species, specific metal, concentration, soil composition, as many heavy metals are considered to be essential for plant growth. Were provided data and reviews regarding the effect of heavy metals on nitrogen metabolism of plants and the responses of plants and the cross-talk of heavy metals and various stressors factors. Is clear to understand the relation between metals amount and the benefit or harm caused on plants, determining then, which mechanism should be activated to protect your physiological system.",book:{id:"10360",slug:"nitrogen-in-agriculture-physiological-agricultural-and-ecological-aspects",title:"Nitrogen in Agriculture",fullTitle:"Nitrogen in Agriculture - Physiological, Agricultural and Ecological Aspects"},signatures:"Vitor Nascimento, Glauco Nogueira, Gabriel Monteiro, Waldemar Júnior, Joze Melissa Nunes de Freitas and Cândido Neto",authors:[{id:"332095",title:"Dr.",name:"Cândido",middleName:null,surname:"Neto",slug:"candido-neto",fullName:"Cândido Neto"},{id:"332157",title:"Prof.",name:"Joze",middleName:null,surname:"Freitas",slug:"joze-freitas",fullName:"Joze Freitas"}]}],onlineFirstChaptersFilter:{topicId:"28",limit:6,offset:0},onlineFirstChaptersCollection:[],onlineFirstChaptersTotal:0},preDownload:{success:null,errors:{}},subscriptionForm:{success:null,errors:{}},aboutIntechopen:{},privacyPolicy:{},peerReviewing:{},howOpenAccessPublishingWithIntechopenWorks:{},sponsorshipBooks:{sponsorshipBooks:[],offset:8,limit:8,total:0},allSeries:{pteSeriesList:[{id:"14",title:"Artificial Intelligence",numberOfPublishedBooks:9,numberOfPublishedChapters:87,numberOfOpenTopics:6,numberOfUpcomingTopics:0,issn:"2633-1403",doi:"10.5772/intechopen.79920",isOpenForSubmission:!0},{id:"7",title:"Biomedical Engineering",numberOfPublishedBooks:12,numberOfPublishedChapters:98,numberOfOpenTopics:3,numberOfUpcomingTopics:0,issn:"2631-5343",doi:"10.5772/intechopen.71985",isOpenForSubmission:!0}],lsSeriesList:[{id:"11",title:"Biochemistry",numberOfPublishedBooks:27,numberOfPublishedChapters:287,numberOfOpenTopics:4,numberOfUpcomingTopics:0,issn:"2632-0983",doi:"10.5772/intechopen.72877",isOpenForSubmission:!0},{id:"25",title:"Environmental Sciences",numberOfPublishedBooks:1,numberOfPublishedChapters:9,numberOfOpenTopics:4,numberOfUpcomingTopics:0,issn:"2754-6713",doi:"10.5772/intechopen.100362",isOpenForSubmission:!0},{id:"10",title:"Physiology",numberOfPublishedBooks:11,numberOfPublishedChapters:139,numberOfOpenTopics:4,numberOfUpcomingTopics:0,issn:"2631-8261",doi:"10.5772/intechopen.72796",isOpenForSubmission:!0}],hsSeriesList:[{id:"3",title:"Dentistry",numberOfPublishedBooks:8,numberOfPublishedChapters:129,numberOfOpenTopics:0,numberOfUpcomingTopics:2,issn:"2631-6218",doi:"10.5772/intechopen.71199",isOpenForSubmission:!1},{id:"6",title:"Infectious Diseases",numberOfPublishedBooks:13,numberOfPublishedChapters:107,numberOfOpenTopics:3,numberOfUpcomingTopics:1,issn:"2631-6188",doi:"10.5772/intechopen.71852",isOpenForSubmission:!0},{id:"13",title:"Veterinary Medicine and Science",numberOfPublishedBooks:10,numberOfPublishedChapters:103,numberOfOpenTopics:3,numberOfUpcomingTopics:0,issn:"2632-0517",doi:"10.5772/intechopen.73681",isOpenForSubmission:!0}],sshSeriesList:[{id:"22",title:"Business, Management and Economics",numberOfPublishedBooks:1,numberOfPublishedChapters:12,numberOfOpenTopics:2,numberOfUpcomingTopics:1,issn:null,doi:"10.5772/intechopen.100359",isOpenForSubmission:!0},{id:"23",title:"Education and Human Development",numberOfPublishedBooks:0,numberOfPublishedChapters:0,numberOfOpenTopics:2,numberOfUpcomingTopics:0,issn:null,doi:"10.5772/intechopen.100360",isOpenForSubmission:!1},{id:"24",title:"Sustainable Development",numberOfPublishedBooks:0,numberOfPublishedChapters:10,numberOfOpenTopics:4,numberOfUpcomingTopics:1,issn:null,doi:"10.5772/intechopen.100361",isOpenForSubmission:!0}],testimonialsList:[{id:"13",text:"The collaboration with and support of the technical staff of IntechOpen is fantastic. 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His research interests and specialties include financial econometrics, financial economics, international economics and finance, housing markets, financial markets, among others.",institutionString:null,institution:{name:"University of Southampton",institutionURL:null,country:{name:"United Kingdom"}}},editorTwo:null,editorThree:null},subseries:{paginationCount:3,paginationItems:[{id:"7",title:"Bioinformatics and Medical Informatics",coverUrl:"https://cdn.intechopen.com/series_topics/covers/7.jpg",isOpenForSubmission:!0,annualVolume:11403,editor:{id:"351533",title:"Dr.",name:"Slawomir",middleName:null,surname:"Wilczynski",slug:"slawomir-wilczynski",fullName:"Slawomir Wilczynski",profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0033Y000035U1loQAC/Profile_Picture_1630074514792",biography:"Professor Sławomir Wilczyński, Head of the Chair of Department of Basic Biomedical Sciences, Faculty of Pharmaceutical Sciences, Medical University of Silesia in Katowice, Poland. His research interests are focused on modern imaging methods used in medicine and pharmacy, including in particular hyperspectral imaging, dynamic thermovision analysis, high-resolution ultrasound, as well as other techniques such as EPR, NMR and hemispheric directional reflectance. Author of over 100 scientific works, patents and industrial designs. Expert of the Polish National Center for Research and Development, Member of the Investment Committee in the Bridge Alfa NCBiR program, expert of the Polish Ministry of Funds and Regional Policy, Polish Medical Research Agency. Editor-in-chief of the journal in the field of aesthetic medicine and dermatology - Aesthetica.",institutionString:null,institution:{name:"Medical University of Silesia",institutionURL:null,country:{name:"Poland"}}},editorTwo:null,editorThree:null},{id:"8",title:"Bioinspired Technology and Biomechanics",coverUrl:"https://cdn.intechopen.com/series_topics/covers/8.jpg",isOpenForSubmission:!0,annualVolume:11404,editor:{id:"144937",title:"Prof.",name:"Adriano",middleName:"De Oliveira",surname:"Andrade",slug:"adriano-andrade",fullName:"Adriano Andrade",profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0030O00002bRC8QQAW/Profile_Picture_1625219101815",biography:"Dr. Adriano de Oliveira Andrade graduated in Electrical Engineering at the Federal University of Goiás (Brazil) in 1997. He received his MSc and PhD in Biomedical Engineering respectively from the Federal University of Uberlândia (UFU, Brazil) in 2000 and from the University of Reading (UK) in 2005. He completed a one-year Post-Doctoral Fellowship awarded by the DFAIT (Foreign Affairs and International Trade Canada) at the Institute of Biomedical Engineering of the University of New Brunswick (Canada) in 2010. Currently, he is Professor in the Faculty of Electrical Engineering (UFU). He has authored and co-authored more than 200 peer-reviewed publications in Biomedical Engineering. He has been a researcher of The National Council for Scientific and Technological Development (CNPq-Brazil) since 2009. He has served as an ad-hoc consultant for CNPq, CAPES (Coordination for the Improvement of Higher Education Personnel), FINEP (Brazilian Innovation Agency), and other funding bodies on several occasions. He was the Secretary of the Brazilian Society of Biomedical Engineering (SBEB) from 2015 to 2016, President of SBEB (2017-2018) and Vice-President of SBEB (2019-2020). He was the head of the undergraduate program in Biomedical Engineering of the Federal University of Uberlândia (2015 - June/2019) and the head of the Centre for Innovation and Technology Assessment in Health (NIATS/UFU) since 2010. He is the head of the Postgraduate Program in Biomedical Engineering (UFU, July/2019 - to date). He was the secretary of the Parkinson's Disease Association of Uberlândia (2018-2019). Dr. Andrade's primary area of research is focused towards getting information from the neuromuscular system to understand its strategies of organization, adaptation and controlling in the context of motor neuron diseases. His research interests include Biomedical Signal Processing and Modelling, Assistive Technology, Rehabilitation Engineering, Neuroengineering and Parkinson's Disease.",institutionString:null,institution:{name:"Federal University of Uberlândia",institutionURL:null,country:{name:"Brazil"}}},editorTwo:null,editorThree:null},{id:"9",title:"Biotechnology - Biosensors, Biomaterials and Tissue Engineering",coverUrl:"https://cdn.intechopen.com/series_topics/covers/9.jpg",isOpenForSubmission:!0,annualVolume:11405,editor:{id:"126286",title:"Dr.",name:"Luis",middleName:"Jesús",surname:"Villarreal-Gómez",slug:"luis-villarreal-gomez",fullName:"Luis Villarreal-Gómez",profilePictureURL:"https://mts.intechopen.com/storage/users/126286/images/system/126286.jpg",biography:"Dr. Luis Villarreal is a research professor from the Facultad de Ciencias de la Ingeniería y Tecnología, Universidad Autónoma de Baja California, Tijuana, Baja California, México. Dr. Villarreal is the editor in chief and founder of the Revista de Ciencias Tecnológicas (RECIT) (https://recit.uabc.mx/) and is a member of several editorial and reviewer boards for numerous international journals. He has published more than thirty international papers and reviewed more than ninety-two manuscripts. His research interests include biomaterials, nanomaterials, bioengineering, biosensors, drug delivery systems, and tissue engineering.",institutionString:null,institution:{name:"Autonomous University of Baja California",institutionURL:null,country:{name:"Mexico"}}},editorTwo:null,editorThree:null}]},overviewPageOFChapters:{paginationCount:4,paginationItems:[{id:"81821",title:"Pneumococcal Carriage in Jordanian Children and the Importance of Vaccination",doi:"10.5772/intechopen.104999",signatures:"Adnan Al-Lahham",slug:"pneumococcal-carriage-in-jordanian-children-and-the-importance-of-vaccination",totalDownloads:0,totalCrossrefCites:0,totalDimensionsCites:0,authors:null,book:{title:"Streptococcal Infections",coverURL:"https://cdn.intechopen.com/books/images_new/10828.jpg",subseries:{id:"3",title:"Bacterial Infectious Diseases"}}},{id:"81813",title:"Schistosomiasis: Discovery of New Molecules for Disease Treatment and Vaccine Development",doi:"10.5772/intechopen.104738",signatures:"Andressa Barban do Patrocinio",slug:"schistosomiasis-discovery-of-new-molecules-for-disease-treatment-and-vaccine-development",totalDownloads:4,totalCrossrefCites:0,totalDimensionsCites:0,authors:null,book:{title:"New Horizons for Schistosomiasis Research",coverURL:"https://cdn.intechopen.com/books/images_new/10829.jpg",subseries:{id:"5",title:"Parasitic Infectious Diseases"}}},{id:"81644",title:"Perspective Chapter: Ethics of Using Placebo Controlled Trials for Covid-19 Vaccine Development in Vulnerable Populations",doi:"10.5772/intechopen.104776",signatures:"Lesley Burgess, Jurie Jordaan and Matthew Wilson",slug:"perspective-chapter-ethics-of-using-placebo-controlled-trials-for-covid-19-vaccine-development-in-vu",totalDownloads:5,totalCrossrefCites:0,totalDimensionsCites:0,authors:null,book:{title:"SARS-CoV-2 Variants - Two Years After",coverURL:"https://cdn.intechopen.com/books/images_new/11573.jpg",subseries:{id:"6",title:"Viral Infectious Diseases"}}},{id:"80546",title:"Streptococcal Skin and Skin-Structure Infections",doi:"10.5772/intechopen.102894",signatures:"Alwyn Rapose",slug:"streptococcal-skin-and-skin-structure-infections",totalDownloads:48,totalCrossrefCites:0,totalDimensionsCites:0,authors:null,book:{title:"Streptococcal Infections",coverURL:"https://cdn.intechopen.com/books/images_new/10828.jpg",subseries:{id:"3",title:"Bacterial Infectious Diseases"}}}]},overviewPagePublishedBooks:{paginationCount:13,paginationItems:[{type:"book",id:"6667",title:"Influenza",subtitle:"Therapeutics and Challenges",coverURL:"https://cdn.intechopen.com/books/images_new/6667.jpg",slug:"influenza-therapeutics-and-challenges",publishedDate:"September 19th 2018",editedByType:"Edited by",bookSignature:"Shailendra K. Saxena",hash:"105e347b2d5dbbe6b593aceffa051efa",volumeInSeries:1,fullTitle:"Influenza - Therapeutics and Challenges",editors:[{id:"158026",title:"Prof.",name:"Shailendra K.",middleName:null,surname:"Saxena",slug:"shailendra-k.-saxena",fullName:"Shailendra K. Saxena",profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0030O00002bRET3QAO/Profile_Picture_2022-05-10T10:10:26.jpeg",biography:"Professor Dr. Shailendra K. Saxena is a vice dean and professor at King George's Medical University, Lucknow, India. His research interests involve understanding the molecular mechanisms of host defense during human viral infections and developing new predictive, preventive, and therapeutic strategies for them using Japanese encephalitis virus (JEV), HIV, and emerging viruses as a model via stem cell and cell culture technologies. His research work has been published in various high-impact factor journals (Science, PNAS, Nature Medicine) with a high number of citations. He has received many awards and honors in India and abroad including various Young Scientist Awards, BBSRC India Partnering Award, and Dr. JC Bose National Award of Department of Biotechnology, Min. of Science and Technology, Govt. of India. Dr. Saxena is a fellow of various international societies/academies including the Royal College of Pathologists, United Kingdom; Royal Society of Medicine, London; Royal Society of Biology, United Kingdom; Royal Society of Chemistry, London; and Academy of Translational Medicine Professionals, Austria. He was named a Global Leader in Science by The Scientist. He is also an international opinion leader/expert in vaccination for Japanese encephalitis by IPIC (UK).",institutionString:"King George's Medical University",institution:{name:"King George's Medical University",institutionURL:null,country:{name:"India"}}}]},{type:"book",id:"7064",title:"Current Perspectives in Human Papillomavirus",subtitle:null,coverURL:"https://cdn.intechopen.com/books/images_new/7064.jpg",slug:"current-perspectives-in-human-papillomavirus",publishedDate:"May 2nd 2019",editedByType:"Edited by",bookSignature:"Shailendra K. Saxena",hash:"d92a4085627bab25ddc7942fbf44cf05",volumeInSeries:2,fullTitle:"Current Perspectives in Human Papillomavirus",editors:[{id:"158026",title:"Prof.",name:"Shailendra K.",middleName:null,surname:"Saxena",slug:"shailendra-k.-saxena",fullName:"Shailendra K. Saxena",profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0030O00002bRET3QAO/Profile_Picture_2022-05-10T10:10:26.jpeg",biography:"Professor Dr. Shailendra K. Saxena is a vice dean and professor at King George's Medical University, Lucknow, India. His research interests involve understanding the molecular mechanisms of host defense during human viral infections and developing new predictive, preventive, and therapeutic strategies for them using Japanese encephalitis virus (JEV), HIV, and emerging viruses as a model via stem cell and cell culture technologies. His research work has been published in various high-impact factor journals (Science, PNAS, Nature Medicine) with a high number of citations. He has received many awards and honors in India and abroad including various Young Scientist Awards, BBSRC India Partnering Award, and Dr. JC Bose National Award of Department of Biotechnology, Min. of Science and Technology, Govt. of India. Dr. Saxena is a fellow of various international societies/academies including the Royal College of Pathologists, United Kingdom; Royal Society of Medicine, London; Royal Society of Biology, United Kingdom; Royal Society of Chemistry, London; and Academy of Translational Medicine Professionals, Austria. He was named a Global Leader in Science by The Scientist. He is also an international opinion leader/expert in vaccination for Japanese encephalitis by IPIC (UK).",institutionString:"King George's Medical University",institution:{name:"King George's Medical University",institutionURL:null,country:{name:"India"}}}]},{type:"book",id:"7123",title:"Current Topics in Neglected Tropical Diseases",subtitle:null,coverURL:"https://cdn.intechopen.com/books/images_new/7123.jpg",slug:"current-topics-in-neglected-tropical-diseases",publishedDate:"December 4th 2019",editedByType:"Edited by",bookSignature:"Alfonso J. 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He is a vice-president of the Latin American Society for Travel Medicine (SLAMVI) and a Member of the Council of the International Society for Infectious Diseases (ISID). Since 2014, he has been recognized as a Senior Researcher, at the Ministry of Science of Colombia. He is a professor at the Faculty of Medicine of the Fundacion Universitaria Autonoma de las Americas, in Pereira, Risaralda, Colombia. He is an External Professor, Master in Research on Tropical Medicine and International Health, Universitat de Barcelona, Spain. He is also a professor at the Master in Clinical Epidemiology and Biostatistics, Universidad Científica del Sur, Lima, Peru. In 2021 he has been awarded the “Raul Isturiz Award” Medal of the API. Also, in 2021, he was awarded with the “Jose Felix Patiño” Asclepius Staff Medal of the Colombian Medical College, due to his scientific contributions to COVID-19 during the pandemic. 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He obtained a Master’s degree in Public Health and PhD in Public Health and Epidemiology. He has a background in Clinical Medicine and has taken courses at higher diploma levels in public health from University of Transkei, Republic of South Africa, and African Medical and Research Foundation (AMREF) in Nairobi, Kenya. Dr. Kasenga worked in different places in and outside Malawi, and has held various positions, such as Licensed Medical Officer, HIV/AIDS Programme Officer, HIV/AIDS resource person in the International Department of Diakonhjemet College, Oslo, Norway. He also managed an Integrated HIV/AIDS Prevention programme for over 5 years. He is currently working as a Director for the Health Ministries Department of Malawi Union of the Seventh Day Adventist Church. Dr. Kasenga has published over 5 articles on HIV/AIDS issues focusing on Prevention of Mother to Child Transmission of HIV (PMTCT), including a book chapter on HIV testing counseling (currently in press). 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His research interest focuses on computational chemistry and molecular modeling of diverse systems of pharmacological, food, and alternative energy interests by resorting to DFT and Conceptual DFT. He has authored a coauthored more than 255 peer-reviewed papers, 32 book chapters, and 2 edited books. He has delivered speeches at many international and domestic conferences. He serves as a reviewer for more than eighty international journals, books, and research proposals as well as an editor for special issues of renowned scientific journals.",institutionString:"Centro de Investigación en Materiales Avanzados",institution:{name:"Centro de Investigación en Materiales Avanzados",country:{name:"Mexico"}}},{id:"76477",title:"Prof.",name:"Mirza",middleName:null,surname:"Hasanuzzaman",slug:"mirza-hasanuzzaman",fullName:"Mirza Hasanuzzaman",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/76477/images/system/76477.png",biography:"Dr. Mirza Hasanuzzaman is a Professor of Agronomy at Sher-e-Bangla Agricultural University, Bangladesh. He received his Ph.D. in Plant Stress Physiology and Antioxidant Metabolism from Ehime University, Japan, with a scholarship from the Japanese Government (MEXT). Later, he completed his postdoctoral research at the Center of Molecular Biosciences, University of the Ryukyus, Japan, as a recipient of the Japan Society for the Promotion of Science (JSPS) postdoctoral fellowship. He was also the recipient of the Australian Government Endeavour Research Fellowship for postdoctoral research as an adjunct senior researcher at the University of Tasmania, Australia. Dr. Hasanuzzaman’s current work is focused on the physiological and molecular mechanisms of environmental stress tolerance. Dr. Hasanuzzaman has published more than 150 articles in peer-reviewed journals. He has edited ten books and written more than forty book chapters on important aspects of plant physiology, plant stress tolerance, and crop production. According to Scopus, Dr. Hasanuzzaman’s publications have received more than 10,500 citations with an h-index of 53. He has been named a Highly Cited Researcher by Clarivate. He is an editor and reviewer for more than fifty peer-reviewed international journals and was a recipient of the “Publons Peer Review Award” in 2017, 2018, and 2019. He has been honored by different authorities for his outstanding performance in various fields like research and education, and he has received the World Academy of Science Young Scientist Award (2014) and the University Grants Commission (UGC) Award 2018. He is a fellow of the Bangladesh Academy of Sciences (BAS) and the Royal Society of Biology.",institutionString:"Sher-e-Bangla Agricultural University",institution:{name:"Sher-e-Bangla Agricultural University",country:{name:"Bangladesh"}}},{id:"187859",title:"Prof.",name:"Kusal",middleName:"K.",surname:"Das",slug:"kusal-das",fullName:"Kusal Das",position:null,profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0030O00002bSBDeQAO/Profile_Picture_1623411145568",biography:"Kusal K. Das is a Distinguished Chair Professor of Physiology, Shri B. M. Patil Medical College and Director, Centre for Advanced Medical Research (CAMR), BLDE (Deemed to be University), Vijayapur, Karnataka, India. Dr. Das did his M.S. and Ph.D. in Human Physiology from the University of Calcutta, Kolkata. His area of research is focused on understanding of molecular mechanisms of heavy metal activated low oxygen sensing pathways in vascular pathophysiology. He has invented a new method of estimation of serum vitamin E. His expertise in critical experimental protocols on vascular functions in experimental animals was well documented by his quality of publications. He was a Visiting Professor of Medicine at University of Leeds, United Kingdom (2014-2016) and Tulane University, New Orleans, USA (2017). For his immense contribution in medical research Ministry of Science and Technology, Government of India conferred him 'G.P. Chatterjee Memorial Research Prize-2019” and he is also the recipient of 'Dr.Raja Ramanna State Scientist Award 2015” by Government of Karnataka. He is a Fellow of the Royal Society of Biology (FRSB), London and Honorary Fellow of Karnataka Science and Technology Academy, Department of Science and Technology, Government of Karnataka.",institutionString:"BLDE (Deemed to be University), India",institution:null},{id:"243660",title:"Dr.",name:"Mallanagouda Shivanagouda",middleName:null,surname:"Biradar",slug:"mallanagouda-shivanagouda-biradar",fullName:"Mallanagouda Shivanagouda Biradar",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/243660/images/system/243660.jpeg",biography:"M. S. Biradar is Vice Chancellor and Professor of Medicine of\nBLDE (Deemed to be University), Vijayapura, Karnataka, India.\nHe obtained his MD with a gold medal in General Medicine and\nhas devoted himself to medical teaching, research, and administrations. He has also immensely contributed to medical research\non vascular medicine, which is reflected by his numerous publications including books and book chapters. Professor Biradar was\nalso Visiting Professor at Tulane University School of Medicine, New Orleans, USA.",institutionString:"BLDE (Deemed to be University)",institution:{name:"BLDE University",country:{name:"India"}}},{id:"289796",title:"Dr.",name:"Swastika",middleName:null,surname:"Das",slug:"swastika-das",fullName:"Swastika Das",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/289796/images/system/289796.jpeg",biography:"Swastika N. Das is Professor of Chemistry at the V. P. Dr. P. G.\nHalakatti College of Engineering and Technology, BLDE (Deemed\nto be University), Vijayapura, Karnataka, India. She obtained an\nMSc, MPhil, and PhD in Chemistry from Sambalpur University,\nOdisha, India. Her areas of research interest are medicinal chemistry, chemical kinetics, and free radical chemistry. She is a member\nof the investigators who invented a new modified method of estimation of serum vitamin E. She has authored numerous publications including book\nchapters and is a mentor of doctoral curriculum at her university.",institutionString:"BLDEA’s V.P.Dr.P.G.Halakatti College of Engineering & Technology",institution:{name:"BLDE University",country:{name:"India"}}},{id:"248459",title:"Dr.",name:"Akikazu",middleName:null,surname:"Takada",slug:"akikazu-takada",fullName:"Akikazu Takada",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/248459/images/system/248459.png",biography:"Akikazu Takada was born in Japan, 1935. After graduation from\nKeio University School of Medicine and finishing his post-graduate studies, he worked at Roswell Park Memorial Institute NY,\nUSA. He then took a professorship at Hamamatsu University\nSchool of Medicine. In thrombosis studies, he found the SK\npotentiator that enhances plasminogen activation by streptokinase. He is very much interested in simultaneous measurements\nof fatty acids, amino acids, and tryptophan degradation products. By using fatty\nacid analyses, he indicated that plasma levels of trans-fatty acids of old men were\nfar higher in the US than Japanese men. . He also showed that eicosapentaenoic acid\n(EPA) and docosahexaenoic acid (DHA) levels are higher, and arachidonic acid\nlevels are lower in Japanese than US people. By using simultaneous LC/MS analyses\nof plasma levels of tryptophan metabolites, he recently found that plasma levels of\nserotonin, kynurenine, or 5-HIAA were higher in patients of mono- and bipolar\ndepression, which are significantly different from observations reported before. In\nview of recent reports that plasma tryptophan metabolites are mainly produced by\nmicrobiota. He is now working on the relationships between microbiota and depression or autism.",institutionString:"Hamamatsu University School of Medicine",institution:{name:"Hamamatsu University School of Medicine",country:{name:"Japan"}}},{id:"137240",title:"Prof.",name:"Mohammed",middleName:null,surname:"Khalid",slug:"mohammed-khalid",fullName:"Mohammed Khalid",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/137240/images/system/137240.png",biography:"Mohammed Khalid received his B.S. degree in chemistry in 2000 and Ph.D. degree in physical chemistry in 2007 from the University of Khartoum, Sudan. He moved to School of Chemistry, Faculty of Science, University of Sydney, Australia in 2009 and joined Dr. Ron Clarke as a postdoctoral fellow where he worked on the interaction of ATP with the phosphoenzyme of the Na+/K+-ATPase and dual mechanisms of allosteric acceleration of the Na+/K+-ATPase by ATP; then he went back to Department of Chemistry, University of Khartoum as an assistant professor, and in 2014 he was promoted as an associate professor. In 2011, he joined the staff of Department of Chemistry at Taif University, Saudi Arabia, where he is currently an assistant professor. His research interests include the following: P-Type ATPase enzyme kinetics and mechanisms, kinetics and mechanisms of redox reactions, autocatalytic reactions, computational enzyme kinetics, allosteric acceleration of P-type ATPases by ATP, exploring of allosteric sites of ATPases, and interaction of ATP with ATPases located in cell membranes.",institutionString:"Taif University",institution:{name:"Taif University",country:{name:"Saudi Arabia"}}},{id:"63810",title:"Prof.",name:"Jorge",middleName:null,surname:"Morales-Montor",slug:"jorge-morales-montor",fullName:"Jorge Morales-Montor",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/63810/images/system/63810.png",biography:"Dr. Jorge Morales-Montor was recognized with the Lola and Igo Flisser PUIS Award for best graduate thesis at the national level in the field of parasitology. He received a fellowship from the Fogarty Foundation to perform postdoctoral research stay at the University of Georgia. He has 153 journal articles to his credit. He has also edited several books and published more than fifty-five book chapters. He is a member of the Mexican Academy of Sciences, Latin American Academy of Sciences, and the National Academy of Medicine. He has received more than thirty-five awards and has supervised numerous bachelor’s, master’s, and Ph.D. students. Dr. Morales-Montor is the past president of the Mexican Society of Parasitology.",institutionString:"National Autonomous University of Mexico",institution:{name:"National Autonomous University of Mexico",country:{name:"Mexico"}}},{id:"217215",title:"Dr.",name:"Palash",middleName:null,surname:"Mandal",slug:"palash-mandal",fullName:"Palash Mandal",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/217215/images/system/217215.jpeg",biography:null,institutionString:"Charusat University",institution:null},{id:"49739",title:"Dr.",name:"Leszek",middleName:null,surname:"Szablewski",slug:"leszek-szablewski",fullName:"Leszek Szablewski",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/49739/images/system/49739.jpg",biography:"Leszek Szablewski is a professor of medical sciences. He received his M.S. in the Faculty of Biology from the University of Warsaw and his PhD degree from the Institute of Experimental Biology Polish Academy of Sciences. He habilitated in the Medical University of Warsaw, and he obtained his degree of Professor from the President of Poland. Professor Szablewski is the Head of Chair and Department of General Biology and Parasitology, Medical University of Warsaw. Professor Szablewski has published over 80 peer-reviewed papers in journals such as Journal of Alzheimer’s Disease, Biochim. Biophys. Acta Reviews of Cancer, Biol. Chem., J. Biomed. Sci., and Diabetes/Metabol. Res. Rev, Endocrine. He is the author of two books and four book chapters. He has edited four books, written 15 scripts for students, is the ad hoc reviewer of over 30 peer-reviewed journals, and editorial member of peer-reviewed journals. Prof. Szablewski’s research focuses on cell physiology, genetics, and pathophysiology. He works on the damage caused by lack of glucose homeostasis and changes in the expression and/or function of glucose transporters due to various diseases. He has given lectures, seminars, and exercises for students at the Medical University.",institutionString:"Medical University of Warsaw",institution:{name:"Medical University of Warsaw",country:{name:"Poland"}}},{id:"173123",title:"Dr.",name:"Maitham",middleName:null,surname:"Khajah",slug:"maitham-khajah",fullName:"Maitham Khajah",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/173123/images/system/173123.jpeg",biography:"Dr. Maitham A. Khajah received his degree in Pharmacy from Faculty of Pharmacy, Kuwait University, in 2003 and obtained his PhD degree in December 2009 from the University of Calgary, Canada (Gastrointestinal Science and Immunology). Since January 2010 he has been assistant professor in Kuwait University, Faculty of Pharmacy, Department of Pharmacology and Therapeutics. His research interest are molecular targets for the treatment of inflammatory bowel disease (IBD) and the mechanisms responsible for immune cell chemotaxis. He cosupervised many students for the MSc Molecular Biology Program, College of Graduate Studies, Kuwait University. Ever since joining Kuwait University in 2010, he got various grants as PI and Co-I. He was awarded the Best Young Researcher Award by Kuwait University, Research Sector, for the Year 2013–2014. He was a member in the organizing committee for three conferences organized by Kuwait University, Faculty of Pharmacy, as cochair and a member in the scientific committee (the 3rd, 4th, and 5th Kuwait International Pharmacy Conference).",institutionString:"Kuwait University",institution:{name:"Kuwait University",country:{name:"Kuwait"}}},{id:"195136",title:"Dr.",name:"Aya",middleName:null,surname:"Adel",slug:"aya-adel",fullName:"Aya Adel",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/195136/images/system/195136.jpg",biography:"Dr. Adel works as an Assistant Lecturer in the unit of Phoniatrics, Department of Otolaryngology, Ain Shams University in Cairo, Egypt. Dr. Adel is especially interested in joint attention and its impairment in autism spectrum disorder",institutionString:"Ain Shams University",institution:{name:"Ain Shams University",country:{name:"Egypt"}}},{id:"94911",title:"Dr.",name:"Boulenouar",middleName:null,surname:"Mesraoua",slug:"boulenouar-mesraoua",fullName:"Boulenouar Mesraoua",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/94911/images/system/94911.png",biography:"Dr Boulenouar Mesraoua is the Associate Professor of Clinical Neurology at Weill Cornell Medical College-Qatar and a Consultant Neurologist at Hamad Medical Corporation at the Neuroscience Department; He graduated as a Medical Doctor from the University of Oran, Algeria; he then moved to Belgium, the City of Liege, for a Residency in Internal Medicine and Neurology at Liege University; after getting the Belgian Board of Neurology (with high marks), he went to the National Hospital for Nervous Diseases, Queen Square, London, United Kingdom for a fellowship in Clinical Neurophysiology, under Pr Willison ; Dr Mesraoua had also further training in Epilepsy and Continuous EEG Monitoring for two years (from 2001-2003) in the Neurophysiology department of Zurich University, Switzerland, under late Pr Hans Gregor Wieser ,an internationally known epileptologist expert. \n\nDr B. Mesraoua is the Director of the Neurology Fellowship Program at the Neurology Section and an active member of the newly created Comprehensive Epilepsy Program at Hamad General Hospital, Doha, Qatar; he is also Assistant Director of the Residency Program at the Qatar Medical School. \nDr B. Mesraoua's main interests are Epilepsy, Multiple Sclerosis, and Clinical Neurology; He is the Chairman and the Organizer of the well known Qatar Epilepsy Symposium, he is running yearly for the past 14 years and which is considered a landmark in the Gulf region; He has also started last year , together with other epileptologists from Qatar, the region and elsewhere, a yearly International Epilepsy School Course, which was attended by many neurologists from the Area.\n\nInternationally, Dr Mesraoua is an active and elected member of the Commission on Eastern Mediterranean Region (EMR ) , a regional branch of the International League Against Epilepsy (ILAE), where he represents the Middle East and North Africa(MENA ) and where he holds the position of chief of the Epilepsy Epidemiology Section; Dr Mesraoua is a member of the American Academy of Neurology, the Europeen Academy of Neurology and the American Epilepsy Society.\n\nDr Mesraoua's main objectives are to encourage frequent gathering of the epileptologists/neurologists from the MENA region and the rest of the world, promote Epilepsy Teaching in the MENA Region, and encourage multicenter studies involving neurologists and epileptologists in the MENA region, particularly epilepsy epidemiological studies. \n\nDr. Mesraoua is the recipient of two research Grants, as the Lead Principal Investigator (750.000 USD and 250.000 USD) from the Qatar National Research Fund (QNRF) and the Hamad Hospital Internal Research Grant (IRGC), on the following topics : “Continuous EEG Monitoring in the ICU “ and on “Alpha-lactoalbumin , proof of concept in the treatment of epilepsy” .Dr Mesraoua is a reviewer for the journal \"seizures\" (Europeen Epilepsy Journal ) as well as dove journals ; Dr Mesraoua is the author and co-author of many peer reviewed publications and four book chapters in the field of Epilepsy and Clinical Neurology",institutionString:"Weill Cornell Medical College in Qatar",institution:{name:"Weill Cornell Medical College in Qatar",country:{name:"Qatar"}}},{id:"282429",title:"Prof.",name:"Covanis",middleName:null,surname:"Athanasios",slug:"covanis-athanasios",fullName:"Covanis Athanasios",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/282429/images/system/282429.jpg",biography:null,institutionString:"Neurology-Neurophysiology Department of the Children Hospital Agia Sophia",institution:null},{id:"190980",title:"Prof.",name:"Marwa",middleName:null,surname:"Mahmoud Saleh",slug:"marwa-mahmoud-saleh",fullName:"Marwa Mahmoud Saleh",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/190980/images/system/190980.jpg",biography:"Professor Marwa Mahmoud Saleh is a doctor of medicine and currently works in the unit of Phoniatrics, Department of Otolaryngology, Ain Shams University in Cairo, Egypt. She got her doctoral degree in 1991 and her doctoral thesis was accomplished in the University of Iowa, United States. Her publications covered a multitude of topics as videokymography, cochlear implants, stuttering, and dysphagia. She has lectured Egyptian phonology for many years. Her recent research interest is joint attention in autism.",institutionString:"Ain Shams University",institution:{name:"Ain Shams University",country:{name:"Egypt"}}},{id:"259190",title:"Dr.",name:"Syed Ali Raza",middleName:null,surname:"Naqvi",slug:"syed-ali-raza-naqvi",fullName:"Syed Ali Raza Naqvi",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/259190/images/system/259190.png",biography:"Dr. Naqvi is a radioanalytical chemist and is working as an associate professor of analytical chemistry in the Department of Chemistry, Government College University, Faisalabad, Pakistan. Advance separation techniques, nuclear analytical techniques and radiopharmaceutical analysis are the main courses that he is teaching to graduate and post-graduate students. In the research area, he is focusing on the development of organic- and biomolecule-based radiopharmaceuticals for diagnosis and therapy of infectious and cancerous diseases. Under the supervision of Dr. Naqvi, three students have completed their Ph.D. degrees and 41 students have completed their MS degrees. He has completed three research projects and is currently working on 2 projects entitled “Radiolabeling of fluoroquinolone derivatives for the diagnosis of deep-seated bacterial infections” and “Radiolabeled minigastrin peptides for diagnosis and therapy of NETs”. He has published about 100 research articles in international reputed journals and 7 book chapters. Pakistan Institute of Nuclear Science & Technology (PINSTECH) Islamabad, Punjab Institute of Nuclear Medicine (PINM), Faisalabad and Institute of Nuclear Medicine and Radiology (INOR) Abbottabad are the main collaborating institutes.",institutionString:"Government College University",institution:{name:"Government College University, Faisalabad",country:{name:"Pakistan"}}},{id:"58390",title:"Dr.",name:"Gyula",middleName:null,surname:"Mozsik",slug:"gyula-mozsik",fullName:"Gyula Mozsik",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/58390/images/system/58390.png",biography:"Gyula Mózsik MD, Ph.D., ScD (med), is an emeritus professor of Medicine at the First Department of Medicine, Univesity of Pécs, Hungary. He was head of this department from 1993 to 2003. His specializations are medicine, gastroenterology, clinical pharmacology, clinical nutrition, and dietetics. His research fields are biochemical pharmacological examinations in the human gastrointestinal (GI) mucosa, mechanisms of retinoids, drugs, capsaicin-sensitive afferent nerves, and innovative pharmacological, pharmaceutical, and nutritional (dietary) research in humans. He has published about 360 peer-reviewed papers, 197 book chapters, 692 abstracts, 19 monographs, and has edited 37 books. He has given about 1120 regular and review lectures. He has organized thirty-eight national and international congresses and symposia. He is the founder of the International Conference on Ulcer Research (ICUR); International Union of Pharmacology, Gastrointestinal Section (IUPHAR-GI); Brain-Gut Society symposiums, and gastrointestinal cytoprotective symposiums. He received the Andre Robert Award from IUPHAR-GI in 2014. Fifteen of his students have been appointed as full professors in Egypt, Cuba, and Hungary.",institutionString:"University of Pécs",institution:{name:"University of Pecs",country:{name:"Hungary"}}},{id:"277367",title:"M.Sc.",name:"Daniel",middleName:"Martin",surname:"Márquez López",slug:"daniel-marquez-lopez",fullName:"Daniel Márquez López",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/277367/images/7909_n.jpg",biography:"Msc Daniel Martin Márquez López has a bachelor degree in Industrial Chemical Engineering, a Master of science degree in the same área and he is a PhD candidate for the Instituto Politécnico Nacional. His Works are realted to the Green chemistry field, biolubricants, biodiesel, transesterification reactions for biodiesel production and the manipulation of oils for therapeutic purposes.",institutionString:null,institution:{name:"Instituto Politécnico Nacional",country:{name:"Mexico"}}},{id:"196544",title:"Prof.",name:"Angel",middleName:null,surname:"Catala",slug:"angel-catala",fullName:"Angel Catala",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/196544/images/system/196544.jpg",biography:"Angel Catalá studied chemistry at Universidad Nacional de La Plata, Argentina, where he received a Ph.D. in Chemistry (Biological Branch) in 1965. From 1964 to 1974, he worked as an Assistant in Biochemistry at the School of Medicine at the same university. From 1974 to 1976, he was a fellow of the National Institutes of Health (NIH) at the University of Connecticut, Health Center, USA. From 1985 to 2004, he served as a Full Professor of Biochemistry at the Universidad Nacional de La Plata. He is a member of the National Research Council (CONICET), Argentina, and the Argentine Society for Biochemistry and Molecular Biology (SAIB). His laboratory has been interested for many years in the lipid peroxidation of biological membranes from various tissues and different species. Dr. Catalá has directed twelve doctoral theses, published more than 100 papers in peer-reviewed journals, several chapters in books, and edited twelve books. He received awards at the 40th International Conference Biochemistry of Lipids 1999 in Dijon, France. He is the winner of the Bimbo Pan-American Nutrition, Food Science and Technology Award 2006 and 2012, South America, Human Nutrition, Professional Category. In 2006, he won the Bernardo Houssay award in pharmacology, in recognition of his meritorious works of research. Dr. Catalá belongs to the editorial board of several journals including Journal of Lipids; International Review of Biophysical Chemistry; Frontiers in Membrane Physiology and Biophysics; World Journal of Experimental Medicine and Biochemistry Research International; World Journal of Biological Chemistry, Diabetes, and the Pancreas; International Journal of Chronic Diseases & Therapy; and International Journal of Nutrition. He is the co-editor of The Open Biology Journal and associate editor for Oxidative Medicine and Cellular Longevity.",institutionString:"Universidad Nacional de La Plata",institution:{name:"National University of La Plata",country:{name:"Argentina"}}},{id:"186585",title:"Dr.",name:"Francisco Javier",middleName:null,surname:"Martin-Romero",slug:"francisco-javier-martin-romero",fullName:"Francisco Javier Martin-Romero",position:null,profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0030O00002bSB3HQAW/Profile_Picture_1631258137641",biography:"Francisco Javier Martín-Romero (Javier) is a Professor of Biochemistry and Molecular Biology at the University of Extremadura, Spain. He is also a group leader at the Biomarkers Institute of Molecular Pathology. Javier received his Ph.D. in 1998 in Biochemistry and Biophysics. At the National Cancer Institute (National Institute of Health, Bethesda, MD) he worked as a research associate on the molecular biology of selenium and its role in health and disease. After postdoctoral collaborations with Carlos Gutierrez-Merino (University of Extremadura, Spain) and Dario Alessi (University of Dundee, UK), he established his own laboratory in 2008. The interest of Javier's lab is the study of cell signaling with a special focus on Ca2+ signaling, and how Ca2+ transport modulates the cytoskeleton, migration, differentiation, cell death, etc. He is especially interested in the study of Ca2+ channels, and the role of STIM1 in the initiation of pathological events.",institutionString:null,institution:{name:"University of Extremadura",country:{name:"Spain"}}},{id:"217323",title:"Prof.",name:"Guang-Jer",middleName:null,surname:"Wu",slug:"guang-jer-wu",fullName:"Guang-Jer Wu",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/217323/images/8027_n.jpg",biography:null,institutionString:null,institution:null},{id:"148546",title:"Dr.",name:"Norma Francenia",middleName:null,surname:"Santos-Sánchez",slug:"norma-francenia-santos-sanchez",fullName:"Norma Francenia Santos-Sánchez",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/148546/images/4640_n.jpg",biography:null,institutionString:null,institution:null},{id:"272889",title:"Dr.",name:"Narendra",middleName:null,surname:"Maddu",slug:"narendra-maddu",fullName:"Narendra Maddu",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/272889/images/10758_n.jpg",biography:null,institutionString:null,institution:null},{id:"242491",title:"Prof.",name:"Angelica",middleName:null,surname:"Rueda",slug:"angelica-rueda",fullName:"Angelica Rueda",position:"Investigador Cinvestav 3B",profilePictureURL:"https://mts.intechopen.com/storage/users/242491/images/6765_n.jpg",biography:null,institutionString:null,institution:null},{id:"88631",title:"Dr.",name:"Ivan",middleName:null,surname:"Petyaev",slug:"ivan-petyaev",fullName:"Ivan Petyaev",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"Lycotec (United Kingdom)",country:{name:"United Kingdom"}}},{id:"423869",title:"Ms.",name:"Smita",middleName:null,surname:"Rai",slug:"smita-rai",fullName:"Smita Rai",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"Integral University",country:{name:"India"}}},{id:"424024",title:"Prof.",name:"Swati",middleName:null,surname:"Sharma",slug:"swati-sharma",fullName:"Swati Sharma",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"Integral University",country:{name:"India"}}},{id:"439112",title:"MSc.",name:"Touseef",middleName:null,surname:"Fatima",slug:"touseef-fatima",fullName:"Touseef Fatima",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"Integral University",country:{name:"India"}}},{id:"424836",title:"Dr.",name:"Orsolya",middleName:null,surname:"Borsai",slug:"orsolya-borsai",fullName:"Orsolya Borsai",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"University of Agricultural Sciences and Veterinary Medicine of Cluj-Napoca",country:{name:"Romania"}}},{id:"422262",title:"Ph.D.",name:"Paola Andrea",middleName:null,surname:"Palmeros-Suárez",slug:"paola-andrea-palmeros-suarez",fullName:"Paola Andrea Palmeros-Suárez",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"University of Guadalajara",country:{name:"Mexico"}}}]}},subseries:{item:{id:"12",type:"subseries",title:"Human Physiology",keywords:"Anatomy, Cells, Organs, Systems, Homeostasis, Functions",scope:"Human physiology is the scientific exploration of the various functions (physical, biochemical, and mechanical properties) of humans, their organs, and their constituent cells. The endocrine and nervous systems play important roles in maintaining homeostasis in the human body. Integration, which is the biological basis of physiology, is achieved through communication between the many overlapping functions of the human body's systems, which takes place through electrical and chemical means. Much of the basis of our knowledge of human physiology has been provided by animal experiments. Because of the close relationship between structure and function, studies in human physiology and anatomy seek to understand the mechanisms that help the human body function. 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His interest later turned to the molecular mechanism and attenuating strategy of sarcopenia (age-related muscle atrophy). His opinion is to attenuate sarcopenia by improving autophagic defects using nutrient- and pharmaceutical-based treatments.",institutionString:null,institution:{name:"Tokyo Institute of Technology",institutionURL:null,country:{name:"Japan"}}},editorTwo:null,editorThree:{id:"331519",title:"Dr.",name:"Kotomi",middleName:null,surname:"Sakai",slug:"kotomi-sakai",fullName:"Kotomi Sakai",profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0033Y000031QtFXQA0/Profile_Picture_1637053227318",biography:"Senior researcher Kotomi Sakai, Ph.D., MPH, works at the Research Organization of Science and Technology in Ritsumeikan University. She is a researcher in the geriatric rehabilitation and public health field. She received Ph.D. from Nihon University and MPH from St.Luke’s International University. 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