\\n\\n
Released this past November, the list is based on data collected from the Web of Science and highlights some of the world’s most influential scientific minds by naming the researchers whose publications over the previous decade have included a high number of Highly Cited Papers placing them among the top 1% most-cited.
\\n\\nWe wish to congratulate all of the researchers named and especially our authors on this amazing accomplishment! We are happy and proud to share in their success!
Note: Edited in March 2021
\\n"}]',published:!0,mainMedia:{caption:"Highly Cited",originalUrl:"/media/original/117"}},components:[{type:"htmlEditorComponent",content:'IntechOpen is proud to announce that 191 of our authors have made the Clarivate™ Highly Cited Researchers List for 2020, ranking them among the top 1% most-cited.
\n\nThroughout the years, the list has named a total of 261 IntechOpen authors as Highly Cited. Of those researchers, 69 have been featured on the list multiple times.
\n\n\n\nReleased this past November, the list is based on data collected from the Web of Science and highlights some of the world’s most influential scientific minds by naming the researchers whose publications over the previous decade have included a high number of Highly Cited Papers placing them among the top 1% most-cited.
\n\nWe wish to congratulate all of the researchers named and especially our authors on this amazing accomplishment! We are happy and proud to share in their success!
Note: Edited in March 2021
\n'}],latestNews:[{slug:"webinar-introduction-to-open-science-wednesday-18-may-1-pm-cest-20220518",title:"Webinar: Introduction to Open Science | Wednesday 18 May, 1 PM CEST"},{slug:"step-in-the-right-direction-intechopen-launches-a-portfolio-of-open-science-journals-20220414",title:"Step in the Right Direction: IntechOpen Launches a Portfolio of Open Science Journals"},{slug:"let-s-meet-at-london-book-fair-5-7-april-2022-olympia-london-20220321",title:"Let’s meet at London Book Fair, 5-7 April 2022, Olympia London"},{slug:"50-books-published-as-part-of-intechopen-and-knowledge-unlatched-ku-collaboration-20220316",title:"50 Books published as part of IntechOpen and Knowledge Unlatched (KU) Collaboration"},{slug:"intechopen-joins-the-united-nations-sustainable-development-goals-publishers-compact-20221702",title:"IntechOpen joins the United Nations Sustainable Development Goals Publishers Compact"},{slug:"intechopen-signs-exclusive-representation-agreement-with-lsr-libros-servicios-y-representaciones-s-a-de-c-v-20211123",title:"IntechOpen Signs Exclusive Representation Agreement with LSR Libros Servicios y Representaciones S.A. de C.V"},{slug:"intechopen-expands-partnership-with-research4life-20211110",title:"IntechOpen Expands Partnership with Research4Life"},{slug:"introducing-intechopen-book-series-a-new-publishing-format-for-oa-books-20210915",title:"Introducing IntechOpen Book Series - A New Publishing Format for OA Books"}]},book:{item:{type:"book",id:"3395",leadTitle:null,fullTitle:"Human Papillomavirus and Related Diseases From Bench to Bedside A Diagnostic and Preventive Perspective",title:"Human Papillomavirus and Related Diseases",subtitle:"From Bench to Bedside - A Diagnostic and Preventive Perspective",reviewType:"peer-reviewed",abstract:"Cervical cancer is the second most prevalent cancer among women worldwide, and infection with Human Papilloma Virus (HPV) has been identified as the causal agent for this condition. 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Pap smear and the recently introduced prophylactic vaccines are the most prominent prevention options, but despite the availability of these primary and secondary screening tools, the global burden of disease is unfortunately still very high \nThis book will focus on the clinical and diagnostic aspects of HPV and related disease, highlighting the latest developments in this field.",isbn:null,printIsbn:"978-953-51-1072-9",pdfIsbn:"978-953-51-7137-9",doi:"10.5772/56594",price:139,priceEur:155,priceUsd:179,slug:"human-papillomavirus-and-related-diseases-from-bench-to-bedside-a-diagnostic-and-preventive-perspective",numberOfPages:336,isOpenForSubmission:!1,isInWos:null,isInBkci:!1,hash:"c6c3820fb6deb675bd38fa1954ec4f56",bookSignature:"Davy Vanden Broeck",publishedDate:"April 30th 2013",coverURL:"https://cdn.intechopen.com/books/images_new/3395.jpg",numberOfDownloads:24985,numberOfWosCitations:5,numberOfCrossrefCitations:5,numberOfCrossrefCitationsByBook:1,numberOfDimensionsCitations:11,numberOfDimensionsCitationsByBook:1,hasAltmetrics:1,numberOfTotalCitations:21,isAvailableForWebshopOrdering:!0,dateEndFirstStepPublish:"May 2nd 2012",dateEndSecondStepPublish:"May 23rd 2012",dateEndThirdStepPublish:"August 27th 2012",dateEndFourthStepPublish:"November 25th 2012",dateEndFifthStepPublish:"December 25th 2012",currentStepOfPublishingProcess:5,indexedIn:"1,2,3,4,5,6",editedByType:"Edited by",kuFlag:!1,featuredMarkup:null,editors:[{id:"93213",title:"Dr.",name:"Davy",middleName:null,surname:"Vanden Broeck",slug:"davy-vanden-broeck",fullName:"Davy Vanden Broeck",profilePictureURL:"https://mts.intechopen.com/storage/users/93213/images/2523_n.jpg",biography:"Prof. Dr. Davy Vanden Broeck, MSc, PhD obtained this MSc degree Biochemistry from Antwerp University (Belgium) with judicium Cum Laude. Afterwards he pursued a PhD in Biomedical Sciences (Antwerp University). Later, he joined the International Centre for Reproductive Health (ICRH) and research efforts focused on sexually transmitted viruses. Finally, he obtained two consecutive post-doc grants at Ghent University (Ghent, Belgium), with specific focus on papilloma virus research.\nCurrently, Dr. Vanden Broeck holds the position of professor Molecular Virology and heads the ICRH HPV/cervical cancer research team. Within this team, multi-disciplinary research is performed on the prevention of cervical cancer (vaccine, screening), as well as clinical/translational aspects of cervical cancer research, but equally fundamental research forms part of the research agenda.",institutionString:null,position:null,outsideEditionCount:0,totalCites:0,totalAuthoredChapters:"1",totalChapterViews:"0",totalEditedBooks:"3",institution:{name:"Ghent University",institutionURL:null,country:{name:"Belgium"}}}],equalEditorOne:null,equalEditorTwo:null,equalEditorThree:null,coeditorOne:null,coeditorTwo:null,coeditorThree:null,coeditorFour:null,coeditorFive:null,topics:[{id:"1079",title:"Genitourinary Oncology",slug:"genitourinary-oncology"}],chapters:[{id:"44399",title:"Molecular Diagnosis of Human Papillomavirus Infections",doi:"10.5772/55706",slug:"molecular-diagnosis-of-human-papillomavirus-infections",totalDownloads:3053,totalCrossrefCites:1,totalDimensionsCites:1,hasAltmetrics:0,abstract:null,signatures:"Santiago 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These compounds are an assorted class of biological macromolecules with amino acid sequence characterized by a unique three-dimensional structure [1]. The three-dimensional structure is not only responsible for the biochemical reactions but also useful in feedback mechanism, transport, and solubility in physiological solutions. Proteins have a variety of important physiological roles, which are due to their ability to specifically bind to respective biological counterparts. Enzymes, hormones, antibodies, globulins, hemoglobin, myoglobin, and numerous lipoproteins are all proteins and peptides involved in catalysis and transport of substances within the body [2].
In 2010, it was reported that around 20 antibody products and 150 protein-based products were approved for use in the US market alone [3]. In that same year, it was reported that >100 approved protein drugs were in use, and ~800 were being developed to treat numerous conditions, including cancer, Alzheimer’s, Huntington’s, and Parkinson’s diseases [4], with worldwide sales figures estimated to be around $70 billion [5]. It is clear that the protein drug class is continuing its strong economic growth, with the global market for bioengineered protein drugs being valued at $151.9 billion in 2013 and expectations that the market could reach $222.7 billion by 2019 (http://www.bccresearch.com/pressroom/bio/global-market-for-bioengineered-protein-drugs-to-reach-$222.7-billion-in-2019). Most of these protein and peptide-based products are still administered by daily or weekly injections [5]. Besides administration route, shelf life imposes a major challenge to the pharmaceutical industry as there are no general rules on how to stabilize protein products and guarantee its safety and activity during the time it is supposed to be marketable [6].
Protein drugs are biopharmaceuticals, which include other biological drugs such as nucleic acid-based drugs, monoclonal antibodies, and recombinant proteins. Although recent advancements in genomics and proteomics have created a large number of protein drug candidates, most fail to be biologically promising
Major obstacles that contribute to low biological activity are low stability, immunogenicity, and toxicity [7]. A combination of these factors results in low plasma half-life, ranging from minutes to several hours, which necessitates repeated administrations, which in turn leads to higher costs and lower patient compliance [7]. To overcome the challenges that protein drugs present, the development of strategies that focus on improving the bioavailability of the drugs by alternative routes of delivery (parenteral, oral, nasal, pulmonary, etc.) and innovative formulation strategies (spray-freeze drying, supercritical fluid methods, fluidized-bed spray coating, lyophilization, jet milling and spray drying) are trending topics in the protein delivery sphere. The aim of these strategies is to improve protein stability during manufacturing, storage and
The use of proteins as therapeutic agents is hampered by their chemical/physical instabilities, low oral bioavailability due to enzymatic degradation in the gastrointestinal tract, low permeability across the epithelial cells lining of the small intestine, and rapid elimination from the circulation. In this section, major obstacles to be overcome in order to successfully deliver protein drugs are examined.
Peptide and protein drugs although generally formulated in solid state still undergo multiple degradative reactions [6]. Chemical degradation involves covalent modification of the primary protein structure via bond cleavage or formation, while physical degradation refers to changes in higher-order structure by denaturation and noncovalent aggregation or precipitation. Physical and chemical types of reactions do not necessarily occur in isolation, but rather one may cause or facilitate the other [7]. Prominent mechanisms of chemical degradation in the solid state include deamidation, oxidation, and the Maillard reaction. Chemical instability due to deamidation has been observed for a number of important proteins, including human growth hormone, recombinant human interleukin-1 receptor antagonists, and recombinant bovine somatotropin [8]. A common deamidation reaction in peptides and proteins in drug formulations is the nonenzymatic intramolecular deamidation reaction of Asn residues. The use of peptide model VYPNGA has led to a better understanding of the Asn deamidation degradative process [8]. By examining the amino acid sequence of a particular peptide or protein with therapeutic potential, residues, which may be susceptible to deamidation, can be identified and formulation decisions made to minimize this type of degradation. The potential for degradative oxidation reactions can be found at various stages of production, packaging, and storage. For instance, peroxide contamination has been found in formulation excipients such as polytethylene glycols and surfactants leading to oxidation of these products [9]. The activation of molecular oxygen to more reactive species requires light or presence of a reducing agent and trace levels of transition metal ions, which can then convert molecular oxygen into more reactive oxidizing species such as superoxide radicals (O2-*), hydroxyl radical (*OH), or hydrogen peroxide (H2O2) [9]. Transition metal ions are often present in excipients, and processing in stainless steel equipment can lead to significant iron contamination [9] and thus represent potential sources, which may contribute to degradative oxidation of peptide or protein drugs. After formulation, the final packaging decision can also have an effect on drug stability. It was demonstrated that even low levels of oxygen (1%) in the vial headspace can result in complete oxidation of a particular product [9]. By understanding the potential sources of contaminants leading to oxidation at all stages of drug production, and the mechanisms by which oxidation reactions take place, formulation strategies can be adopted to minimize these events. For instance, in the process of developing the PTH (1-34) microprojection patch for transdermal delivery, oxidation was identified as the major chemical degradation pathway [10]. It was determined that the addition of 0.03% EDTA to the drug formulation could effectively delay oxidation, which was measured using RP-HPLC. Further, stability testing in the presence and absence of antioxidizing agents and other excipients was performed to assess the compatibility of the patch with packaging components. Indeed, several of the patch components were shown to contribute to volatile compounds, which were chemically and/or physically incompatible with the coated PTH (1-34) formulation. Overall, the selection of appropriate packaging materials and the use of a desiccant sachet in the package appeared to make it possible to achieve the target of 95% PTH (1-34) purity at the end of a two-year shelf life at ambient storage temperature [11]. In some protein formulations, reducing sugars (e.g., fructose, maltose, lactose, glucose, and xylose) react with basic protein residues such as lysine, arginine, asparagine, and glutamine [9]. In a stability study of recombinant human relaxin, it was discovered that the use of glucose as an excipient in a liophilized formulation resulted in covalent adducts of glucose with amino groups on the side chains of the protein formed by Maillard reaction [12]. In this case, switching to the nonreducing sugar (trehalose), or a polyhydric alcohol (mannitol), resulted in greater relaxin stability.
Protein drugs very often undergo physical changes that may result in change of pharmacological effect and potency. Physical instability involves changes in the three-dimensional conformational integrity of the protein and does not necessarily involve covalent modification. These physical processes include denaturation, aggregation, precipitation, and adsorption to surfaces [8]. Protein drugs may undergo these changes during manufacturing, shipping, storage, and administration. Earlier concerns focused on denaturation (unfolding), oxidation, and deamination of protein drugs. Recently, aggregation has emerged as the main problem with protein therapeutics [11]. Protein aggregation is a multistage process that involves unfolding or misfolding of monomeric units of protein along with one or more assembly steps of monomeric protein to form soluble or insoluble oligomers or higher-molecular-weight aggregates [13]. Protein aggregates are often considered ordered if they occur as long, rigid fibrils or filaments. The most characterized aggregation state is the amyloid fibril, associated with neurodegenerative diseases such as Alzheimer’s disease, Parkinson’s disease, and Huntington’s disease [14, 15]. Protein aggregation can be problematic during drug manufacturing, especially if it is insoluble and tends to precipitate, and typically reduces drug stability and shelf life [15]. In worst-case scenarios, aggregation might have an undesirable impact on drug potency, pharmacokinetics, and immunogenicity [16]. Protein aggregation can be triggered by many factors such as shear stress, high temperatures, changes in pH, and high protein concentration [16]. Unfortunately, it is very difficult to predict if the protein drug will undergo aggregation because of the complexity of the mechanism involved in the aggregate formation.
Therapeutic activity of proteins is highly dependent on their conformational structure, which is flexible and sensitive to external conditions such as pH, temperature, and impurities in the excipients [15]. The detection of structural changes in protein is complex in pharmaceutical formulations and is a major challenge for the development and quality of protein drugs [16]. In addition, protein-based drugs have been shown to be immunogenic and in some cases the production of neutralizing antibodies have led to the inhibition of the therapeutic effect [16].
Until recently, injections (i.e., intravenous, intramuscular, or subcutaneous routes) remained the most common means for administering protein drugs. However, the bioavailability of protein drugs using these routes are low due to their rapid elimination from the circulation through renal filtration, enzymatic degradation and uptake by the reticuloendothelial system [17]. Oral dosage is the most attractive route of administration because of the accompanying decreased medical costs and improved patient compliance. However, oral administration of protein drugs results in even lower bioavailability [2]. The main reasons for the low oral bioavailability are the instability of these drugs in the low pH environment of the gastrointestinal tract as well as inactivation and digestion by proteolytic enzymes in the intestinal lumen. In addition, protein drugs have high molecular masses and are hydrophilic, with logP values <0. This means that these drugs are more difficult to transport via the paracellular route across the epithelial cells lining of the small intestine [2, 16].
Despite their many attractive features, protein drugs come with many complications with regards to formulation. Unlike their small molecule drug counterparts, they are often complex molecules with secondary, tertiary, and quaternary structures and generally contain side chains with various chemical properties. The disruption of this complexity can lead to loss of function of the drug. Thus, the formulation of these biological compounds for therapeutic use must maintain their shape and form thus maintaining their activity [2].
Spray-freeze drying was first introduced in 1994, and it was at first classified as a variant of dry milling [18]. Since pharmacological therapeutics have limited stability in liquid solutions, several methods, such as spray-freeze drying and spray drying, have been developed for proper removal of liquids such as water. Spray-freezing involves spraying a solution containing the macromolecule of interest into a vessel containing cryogenic liquid such as oxygen, nitrogen, or argon, which results in freezing of the droplets due to the low boiling point of the cryogenic fluids used [19]. Spray-freeze drying is the sublimation of solid water (ice) following freezing of the solution, and despite its disadvantages, it has become quite an established method in the pharmaceutical industry [20]. The reason for this is quite clear, spray-freeze drying significantly increases the shelf life of pharmaceuticals, it is an extremely sterile process (compared to spray drying), and the product can be readily reconstituted at the time of use. Spray-freeze drying entails three major steps: (1) freezing, the crystallization of water; (2) primary drying, the removal of ice via sublimation; and finally (3) secondary drying, the desorption of residual water from product [19].
Even though this method is used for obtaining protein particles, stresses involved with freezing and drying have been shown to cause irreversible damage to the protein due to degradation, aggregation, and eventual loss of biological activity [19]. Similar to spray drying the majority of the damage occurs in the atomization and freezing of the droplets in the cold vapor phase of the lyophilization process [21].
Supercritical fluids (SCF) are used in variety of extraction and analytical methods. They can also be used for the production of pharmaceutical powders, mainly those intended for inhalation such as inhalation steroids dexamethasone, flunisolide, and triamcinolone acetonide [22]. SCFs have properties of gases and liquids at temperatures and pressures above their critical point. Advantages of SCFs include density values resulting in high dissolving power, lower viscosity levels compared to other liquids, and higher diffusivity allowing high mass transfer [19]. Among present SCFs, CO2 is the most commonly used due to its low critical temperature (31.2°C) and pressure (7.4 MPa); other advantages include nonflammability, nontoxicity, and cost-effectiveness [19].
There are two major principles for particle precipitation when using SCFs. SCFs can be used as (1) solvents (rapid expansion of supercritical solution (RESS) and particles from gas saturated solutions (PGSS)) and (2) antisolvents (gas antisolvent (GAS), aerosol solvent extraction system (ASES), supercritical fluid antisolvent (SAS), precipitation with compressed antisolvent (PCA), and solution enhanced dispersion by supercritical fluids (SEDS)). Since the early 2000s, solutions consisting of proteins along with a cosolvent, such as ethanol, have been precipitated using CO2 [23]. The integrity of such proteins depends on the operating conditions such as temperature, pressure, flow rates, and the concentration of the ingredients used, and by properly optimizing such conditions, the precipitation of proteins using the SCFs, such as CO2, has become a promising method for particle precipitation [24].
Fluidized-bed spray coating is a commonly used method in the pharmaceutical industry for coating of small particles [25]. Coating of particles has several advantages, such as providing acid resistance [24], modifying the release of the particles [26], protecting the therapeutic agent from light, and moisture and masking the taste of a substance [27]. In this process, particles to be coated come in contact with droplets of coating solution after being fluidized via air currents and are then dried using heated air; thus, after several loops through the spraying and drying zones, a uniform coat is achieved [28]. Further, the uniformity and success of the coating is dependent on the spreading of the droplet on the surface of the particle [29].
As a result of recent advancements in fluidized-bed spray coating systems, particles as small as 50 µm can be coated. For instance, fluidized-bed spray coating was applied to recombinant human deoxyribonuclease (rhDNase), and the coating was examined via scanning electron microscopy [30]. The coating demonstrated strong integrity when introduced to mechanical force; however, the process resulted in aggregation of the proteins,, which may be mainly due to the thermal stress involved with the process [29]. Aggregation was significantly reduced however, when rhDNase was formulated with calcium ions, thus suggesting in presence of proper stabilizers fluidized-bed spray coating is a feasible method for coating and preparing dried pharmaceutical proteins [31].
Protein instability is one of the major reasons protein drugs are still administered via injections and not orally. Therefore, in order to overcome this hurdle, proteins must be made into solid forms to achieve an acceptable shelf life [32]. Lyophilization has become one of the most commonly used methods for generating solid protein drugs [33]. Lyophilization consists of three steps beginning with (1) freezing, where the solution that is to be dried is frozen at a controlled rate thus removing water from the protein as ice crystals, at this point ~20% of water remains in a unfrozen phase known as maximal freeze concentrate [31]. Freezing is followed by (2) primary drying, where frozen water is removed via sublimation resulting in significant desorption of water (~10%). The remaining water is removed at higher temperatures in the final stage, (3) secondary drying, via desorption which lowers the fluid moisture content to few tenth of a percent [34].
A variety of stresses caused by lyophilization, such as low temperatures, formation of dendritic ice crystals, pH changes, phase separations, increase in ionic strengths, and removal of protein hydration shell, can result in reversible [33] and irreversible [34] structural changes in the protein [33]. Thus, for proteins that are sensitive to the listed stresses, specific cryo-/lyo-protectants can be used, such as commonly used sugars/polyols, nonaqueous solvents, polymers, protein itself, surfactants, and amino acids [33]. Further, extra effort is made to fully customize the lyophilization cycles in order to avoid lyophilization cycle-related stresses such as freezing rate and temperature, thermal treatment conditions, drying rate and temperature, and final moisture content [33].
Jet milling is a method used for particle size reduction using interparticle collisions and abrasion to produce particles ranging between 1 and 20 µm [19]. Although Jet milling is a great method for particles size reduction (1–20 µm), it does come with some drawbacks, such as lack of control over size, shape, surface properties, and morphology. Furthermore, the high energy input can be detrimental to proteins as it can lead to protein degradation [19]. In a study where horseradish peroxidase was coprecipitated with carbomer and jet milled for two different time points, it was demonstrated that the longer the jet milling process, the more significant the reduction in protein activity [35]. In fact, grinding the power for 10 min in a mortar almost completely eliminated the activity of peroxidase [36] However, pulmonary activity of salmon calcitonin along with a variety of absorption enhancers (oleic acid, lecithin, citric acid, taurocholic acid, dimethyl-beta-cyclodextrin, and octyl-beta-D-glucoside) micronized after freeze drying with lactose showed significant blood levels of calcitonin in rats [37]. Further, it has been suggested that microparticle preparation is possible via melting, pregrinding, and a final jet milling step for particle size reduction [36]. Lastly, as peptides fed into the machine have to be coarse enough to allow for free flow and fine enough not to block the hopper and pipe work, they are at times required to be lyophilized which can result in protein degradation if no lyoprotectant is used [36].
Spray drying is a method used for forming protein particles in lower molecular range [38]. The solution is automatically fed into droplets that rapidly dry due to high surface area and large amount of air–water interfacial area. During the drying process, which can range from 100 milliseconds to seconds, the critical increase in temperature is prevented by the evaporation of the solvent, which results in the temperature of particles remaining significantly lower than the temperature of the gas and drying powder is quickly removed from the drying zone to prevent overheating [25]. Spray drying allows control over a variety of particle design features, including particle size and distribution, surface energy and rugoses, particle density, surface area, porosity, and microviscosity [39]. Since the average radius of particles obtained ranges between 2 and 6 µm, spray drying is generally used for pulmonary particle delivery [40] such as the protein insulin [41].
Although the air-drying process of spray drying prevents thermal degradation of proteins, the atomization process may present a different obstacle. The high shear rate required for the atomization process can lead to degradation of macromolecules. For instance, a study demonstrated degradation of human growth hormone (hGH) during the air–liquid interface following atomization, while the tissue-type plasminogen activator (t-PA) remained intact [42]. There have been several proteins that have been successfully air-dried. Niven et al. spray dried formulations of recombinant human granulocyte colony-stimulating factor (rhG-CSF) [43], and Dalby et al. produced fine protein particles in a process where they combined nebulization, air drying, and electrostatic collection [44].
Another promising approach to enhance the stability of therapeutic peptides and proteins is encapsulation into a micro- or nanoparticle, with the aim of protecting the drug from the hostile environments in the body [45]. At their target location, biodrugs typically are released from the particle by diffusion, swelling, erosion, or degradation [46]. Biological systems are usually protected by nanometer-sized barriers, which are extremely specific with regards to transport of biological molecules. Permeation through such barriers and their access to specific biological compartments is dictated by chemical properties, size, and shape of biological molecules [47]. Nanotechnology, defined as development and application of materials, structures, devices, and systems by modeling and manufacturing of the matter in the nanoscale range (1–100 nm), can be used to provide protection against the degreadation of biological agents [48]. As nanoparticles are similar in scale to biological molecules, nanoparticles can have many medical applications and be engineered to have various functions. As their properties allow them to cross biological barriers, nanoparticles can be used to transport therapeutic molecules to sites of interest, providing access to molecules of interest and thus modulation of molecular interactions [48, 49].
One of the main issues for lack of efficacy for some current therapeutics is the inability to be fully delivered to the required sites, which can be due to their low solubility. Low efficacy may result in increasing dosage, thus correlating with increased side effects [50]. The use of nanocarriers can aid in overcoming some of these obstacles. The surface of nanocarriers usually consists of polymers or biodegradable molecules that are customized to ensure biocompatibility and selective targeting [48]. In fact, nanocarriers may offer numerous advantages over free drugs, such as protecting the drug from premature interaction with unwanted biological entities and degradation, enhancing the absorption of the drug into a specific tissue of interest (cancers or tumors), increasing the pharmacokinetics of the drug, and improving the intracellular penetration of the drug [51].
Nanoparticles and nanocarriers can be used for delivery of peptide drugs to specific sites of interest, avoiding degradation in the GIT and first-pass metabolism via the hepatic route. In fact, peptides have been transported using nanocarriers. Hyaluronic acid–Fe2O3 hybrid magnetic nanoparticles were designed to deliver peptides to HEK293 and A529 cells at a 100% level [52]. Further, functionalized gold nanoparticles consisting of a drug peptide ligand and a targeting peptide were shown to be both effective and enhance the activity and selectivity of such peptide multifunctionalized conjugates [53]. Furthermore, carrier molecules have been shown to increase membrane permeability of protein therapeutics such as insulin, interferon α2b, and human growth hormone through epithelial membrane of small intestine thus increasing the bioavailability of listed protein therapeutics [54].
Proposed in 1970s [55], PEGylation is the attachment of polyethylene glycol to drug molecules as a method of transforming proteins, peptides, small molecules, and oligonucleotides into more potent drugs [56]. PEGylated molecules tend to be more clinically useful compared to their unmodified counterparts as they tend to have higher stability and solubility, longer half-life in the systemic circulation, reduced renal clearance, reduced immunogenicity and antigenicity [57], and higher potency [58].
Protein drugs, such as enzymes, cytokines, and antibodies, have been shown to be significantly improved as a result of PEGylation [59]. Although it is common to see improvements in retention within circulation and reduction of immune response and degradation, the loss of biological activity due to PEGylation is quiet common [60]. The loss of biological activity is however compensated with improved pharmacokinetics as seen in α-interferon Pegasys® [61]. Currently, there are several PEGylated drugs available for public use, including PEG–adenosine deaminase (Adagen®) [62], PEG–asparaginase (Oncaspar®) [63], PEG–interferon α2b (PEG–Intron®) [64], PEG–interferon α2a (Pegasys®) [63], and PEG–growth hormone receptor antagonist (Pegvisomant, Somavert®) [65]. Before PEGylated drugs are made available to public use, they must undergo biological tests to ensure that the advantage of PEGylation does not result in increased toxicity [62].
Numerous strategies have been developed and applied to control or prevent protein aggregation. Protein aggregation can be reduced by introducing disulphide bonds, salt bridges, and metal ions to stabilize and rigidify regions involved in local unfolding. However, extensive clinical trials will be required to confirm if there are any adverse effects associated with these modifications [15, 16]. A more direct approach is to alter the formulation of the protein. One approach to reduce aggregation is to work with protein solutions at lower concentrations and correspondingly larger volumes. A number of excipients have been used with varying success to reduce protein aggregation; however, each has its own limitations [14]. Nonionic detergents can be used to reduce aggregation induced by shear and heat. Cyclodextrins can also be used to reduce aggregation. For example, cyclodextrins suppress the aggregation of insulin. Another approach to reduce aggregation is to use lyophilized dosage forms [16]. Lyophilization is generally regarded as an effective means to stabilize proteins [13, 14]. However, proteins can undergo reversible conformational changes in the lyophilized state, which makes them more susceptible to undesirable side reactions. For example, the aggregation of lyophilized insulin can be ameliorated by the presence of trace moisture [15, 16].
To improve the oral bioavailability of protein drugs, many strategies have been developed. One strategy involves the modulation of the physiochemical properties of the gastrointestinal tract. This could be achieved by the use of protease inhibitors as an additive to reduce the rate of enzymatic degradation [18]. For example, the enzymatic degradation of insulin in the intestine is known to be mediated by the serine proteases trypsin, α-chymotrypsin, and thiol metalloproteinase insulin degrading enzymes. The use of additives that inhibit these enzymes was found to increase the intestinal absorption of insulin by 10% in rats [66]. Also, the modulation of the tight-junction permeability to increase paracellular transport of protein molecules has been studied. However, this approach requires further investigations before it can be applied [18].
Another strategy to improve protein drug bioavailability involves chemical modification of the protein. This includes the synthesis of a protein analog with an improved enzymatic stability and/or membrane penetration. For example, insulin tends to self-associate to form hexamers. The absorption of hexameric insulin is lower than that of the monomeric insulin analog [2]. Mutation of the amino acids that are involved in self-association results in the formation of the monomeric insulin analog known as insulin lispro (Humalog®, Eli Lilly), which is characterized by rapid onset of action following subcutaneous injection [16]. Chemical modification could also be used to produce a prodrug, which could be useful to protect the drugs against enzymatic degradation [18]. The introduction of novel functional groups to protein drugs that are recognized by transporters can also aid in their absorption. For example, adding a dipeptide that is recognized by peptide-influx transporters in the gastrointestinal tract to a protein drug results in significant improvement in its oral bioavailability [16, 18]. Another way to improve protein stability is acylation of the protein drug, which involves the attachment of fatty acids to the exposed residues on the protein surface. This kind of modification increases the affinity of the protein to the serum albumin resulting in an increase in its half-life. Acetylation of insulin led to the development of insulin detemir (Levemir®, Nova Nordisk), which is a long-acting insulin analog [16]. The conjugation of protein drugs with polymers is one of the approaches used to improve the bioavailability of protein drugs. Currently, poly (ethylene glycol) (PEG) is the most widely used polymer. Protein conjugation with PEG reduces the plasma clearance rate by reducing the metabolic degradation [67].
It is also possible to increase the bioavailability of protein drugs by using pharmaceutical technologies. For example, the use of the mucoadhesive delivery system was found to prolong the residence time of protein drug at the local site of absorption and to increase the concentration gradient between delivery system and intestinal membrane, which ultimately results in a higher rate of drug absorption [18]. In addition, protein delivery systems represent an effective method to effectively deliver protein drugs. The most often used delivery systems include liposomes, micelles, microspheres, and hydrogels. The use of carriers provides a higher degree of protection against enzymatic degradation and other destructive factors because the carrier wall completely isolates drug molecules from the environment [18]. Liposomes possess the most suitable characteristics for protein encapsulation. Encapsulating insulin in liposomes results in enhanced oral absorption of insulin [16], [18]. A combination of these approaches can also be used for the development of a successful [16], [18] approach for the delivery of protein drugs, for example, the multifunctional smart polymer that is equipped with a pH-dependent drug release, Ca+2 deprivation ability, and mucoadhesive characteristic. The use of this system to deliver insulin by the oral route results in 10% bioavailability [18].
Currently, the most accepted method of delivery of protein/peptide compounds is the parenteral administration of liquid formulations [68]. This method has become widely accepted by the pharmaceutical companies as it is the fastest way toward achieving commercialization [69]. However, as the therapeutic range of protein/peptide compounds increases, so does the demand for improved formulations. Even though designing novel drug delivery systems is not essential for the success of such compounds, they are important for increased efficacy, patient compliance, and reduced errors in drug administration [20]. Thus, along with parenteral administration of protein/peptide compounds, other routes of delivery such as oral, nasal, pulmonary, ocular, and transdermal delivery have been explored [69].
Parenterally administered protein drugs are most likely to be commercially successful since most animal studies and early clinical trials are performed via direct injections, thus making parenteral drug delivery one of the most popular forms of delivery assuming that injections meet the desired safety and efficacy targets [17]. Drugs delivered parenterally, whether intravenously or intramuscularly, gain full access to the systemic circulation due to rapid drug absorption. The short half-life of peptide drugs within the bloodstream results in repeat doses which correlate with oscillating drug concentrations within the blood [69].
There are numerous injection devices available for patients. For patients with daily injection requirements such as insulin, there are small diameter needle and syringes available. In fact, to improve patients’ quality of life, the patient is now provided with prefilled syringes, syringe injectors, injectors, and pen devices, which may be preloaded with the drug of interest, and autoinjectors are regularly utilized as patients require more flexible and convenient injection devices moving away from the traditional syringe and vial [70]. For instance, insulin is now available in a variety of syringe injectable forms, infusion pumps, jet injectors (a needleless system that transports insulin transcutaneously), and reusable and prefilled pens [70]. All injectable devices must undergo stringent testing to ensure that the patient receives the proper dose of the drug in its expected form. For instance, in needleless systems that depend on high velocity liquid injection, which is dependent on compressed gas, the sheer stress can compromise the configuration of the protein [71, 72].
The rapid absorption of parenterally delivered drug is quickly followed by a rapid decline in the drug levels in the systemic circulation, which can be problematic in cases of chronic conditions where daily or weekly injections may be required for years. The requirement for numerous injections can result in decreased patient compliance, thus resulting in the development of prolonged release parenteral drug delivery systems [71]. These drug delivery systems include use of implants, which are biodegradable drug delivery systems mainly composed of either polylactic acid (PLA) or polyglycolic acid (PLGA) to control the release of the therapeutic drug [73]. However, since implants often require surgery and have been shown to have poor content uniformity in lower drug doses, in situ microparticle systems have been shown to be more advantageous due to the presence of an external oil phase [74]. ISM showed comparable drug release profile to drug release of microparticles prepared by solvent evaporation method, thus potentially becoming an alternative to more complicated microencapsulation methods [75].
One of the major challenges for protein drug delivery via the oral route is the susceptibility of the protein drug to proteolytic degradation in the gastrointestinal tract (GIT), which is at its highest in the stomach and the duodenum of the small intestines and is significantly lower in the mouth, pharynx, esophagus, ileum, and the colon. Another challenge is the bioavailability of the drug, which is dependent on two major factors, the molecular weight (MW) of the drug and its solubility. Bioavailability is essentially independent of MW for drugs less than 700 Da; however, with increasing MW passed this threshold, there is a decrease in the bioavailability of the drug. Drug compounds also need to meet a certain level of hydrophobicity criteria as they are required cross biological membranes. However, most biological drug compounds considered for therapeutic use are frequently greater than 700 Da and are hydrophilic [76]. Thus, degradation and poor absorption are the main bioavailability barriers. There are however suggested methods for increasing the survival of the peptides as it moves through the GIT [75].
There are current methods for increasing the bioavailability of peptidic drugs such as (1) modifying the N- or C-terminus to increase half-life (encephalin, conversion of C-terminal methionine to methioniol group [77]); (2) altering the terminal amino acids from L-amino acid to a D-amino acid (arginine-vasopressin analog 1-deamino-8-D-arginine [77, 78]); (3) converting the linear peptide into a cyclic analog to avoid degradation by carboxy- and amino-peptidases (successfully performed in a model hexapeptide [77]); (4) use of peptidomimetics, which are molecules that mimic the action of peptides but are no longer peptidic in nature and prodrugs, which can be metabolized in the body releasing the therapeutic agent in return; and (5) coadministration of the peptide drug with digestive enzyme inhibitors [79]. The GIT presents both physical and chemical challenges for oral delivery of protein drugs; however, recent developments have made progress in facing each of those challenges and obstacles. Even though the development of new formulation methods, which have shown to improve bioavailability of protein drugs, are still costly, the progress in this field is still quite promising [20].
The use of the nasal cavity as a site for systemic peptide drug delivery has several benefits, such as (1) rapid absorption rate, which in some cases have been shown to be as effective as intravenous injections and require lower doses; (2) high permeability due to the nasal epithelium (up to 1 kDa) [80]; along with (3) high total blood flow; (4) avoidance of first-pass metabolism; and (5) accessibility. The combination of such characteristics allows for a faster onset of pharmacological activity and lower side effects [81]. The olfactory nerves also allow for the direct transport of drug to the brain as the blood–brain barrier provides a challenging obstacle for numerous drugs such as antibiotics, antineoplastic agents, and other drugs that are active in the central nervous system [82].
There are a variety of formulation factors that can affect the absorption of drugs within the nasal cavity. Such factors include dose and volume, pH, osmolarity of the solution which the drug is dissolved in, viscosity, excipients used (such as absorption enhancers), dosage form (spray, powder, or drops), administration techniques (inhalation or mechanically assisted), and devices used to administer the drug [83]. Further, despite the fact that nasally administered drugs are able to avoid first-metabolism, bioavailability of peptide drugs is still limited due to the presence of broad range of metabolic enzymes that reside in the nasal mucosal cavity and the epithelial cell lining [84].
Currently, drugs ranging from small to large macromolecules such as protein drugs, hormones, and vaccines are delivered through the nasal cavity [85]. For instance, in the presence of absorption enhancers, which aid in modulating the nasal epithelium permeability, insulin can be effectively administered through the nasal cavity [84].
The large surface area of the lung along with its well vascularized thin epithelial lining provides a noninvasive method for drug delivery, direct access to systemic circulation, and allows for avoidance of first pass metabolism and GIT degradation [86]. It has been suggested that to achieve successful pulmonary delivery of drug, the drug must reach the alveoli or deep lung; thus, the particle size must range within 1–2 µm for optimum absorption [87]. The inhalation of therapeutics is an effective means for providing therapies for respiratory [88] and a wide range of other disorders [89].
Even though animal studies have shown the bioavailability of drugs delivered via the pulmonary route ranging from ~10% to 50% depending on the type of protein, similar success rates have not been seen in human studies [70]. For instance, pulmonary insulin delivery demonstrated just below 50% bioavailability in animals [90]; bioavailability in humans is merely 10–15% [70]. These findings suggest that the bioavailability of a drug in animals is not necessarily predictive of that of a human. Another obstacle associated with pulmonary delivery is the clinical toxicology of the lungs, particularly when dealing with cytokines and growth factors that may have a local effect on the tissue [70]. The particle size of the drug also plays a critical role in its bioavailability in the lungs [91]. As previously stated, the smaller the particle size, the deeper it will penetrate the lung thus the higher the bioavailability. However, for larger molecular drugs, patients may need to use different dosages and multiple administrations to achieve the desired therapeutic effect [70]. Another challenge for pulmonary delivery of protein drugs is the rapid increase in levels of the drug in the serum, which may not be problematic in cases where the drug has a large margin of safety [89]. Although, this may be desirable for instances where fast delivery of a drug is required, such as insulin preceding a meal, it can result in unwanted side effects and will require more doses to achieve and maintain the required serum levels. However, new technologies, such as rapid-acting, slow-release analogs of drugs, such as insulin, have been developed to allow for an improved pulmonary peptide drug delivery [91].
In order to develop an analog of a protein drug, which can be deemed, therapeutically viable there are a variety of factors that need to be considered. A logical first step would be to gain a full understanding of physiological and chemical barriers, which the protein drug will encounter. Although this field is only a few decades old, significant progress has been made in many areas. There has been an increase in understanding of the advantages and disadvantages of different routes of protein drug delivery. Thus, with proper modifications, such as modifications of the N- or C- terminus, alteration of terminal amino acids, converting the conformation of protein from linear to a circular form, use of peptidomimetics, enzyme inhibitors, or PEGylation, protein drugs can be engineered based on the existing knowledge of proteolytic enzymes, which the protein drug will face once within the systemic circulation. Furthermore, recent advancements in the field of nanomedicine has allowed for the encapsulation of proteins resulting in increased bioavailability. Modifications and new developments in formulation technologies have also allowed for the potential production of protein drugs, which were originally thought to be uneconomical for large-scale production. Proper formulation of the drug product is dependent on choosing the most stable form of the protein drug and fully understanding the chemical and physical properties and the stability of the compound in varying conditions in short and long-term studies.
Pregnancy is a time of transformation for both the mother and the baby, with significant physical and emotional changes. Even in uncomplicated pregnancies, these improvements can impact pregnant women’s quality of life as well as maternal and child health. Women’s wellbeing, as well as their current level of understanding and knowledge, would undoubtedly have a significant impact on society [1]. Pregnant women need health information to improve their self-care skills and increase their empowerment when following preventive health habits. The cardiovascular system undergoes various changes as a result of pregnancy. A normal, healthy pregnant woman’s blood volume rises by nearly 50% over that of a non-pregnant woman. In addition, due to the vascular permeability associated with extreme preeclampsia, efforts to increase blood volume in these patients have been unsuccessful [1, 2]. Pregnancy (critical care scenario) is the reduction in venous return to the heart and decrease in cardiac output associated with the supine position. This effect is obviously more pronounced in the third trimester, when the uterus is largest. The so-called supine hypotensive syndrome.
When treating a critically ill pregnant woman, various hematologic changes must be taken into account. During pregnancy, the thrombocyte count remains largely constant, it leads to thrombocytosis. These improvements, when combined with a decrease in fibrinolysis, lead to the hypercoagulable state of pregnancy. Deep vein thrombosis and pulmonary embolism are five times more common during and immediately after pregnancy [3]. Both the residual volume and the expiratory reserve volume decrease, resulting in an obligate reduction in functional residual capacity. During pregnancy, the vital ability remains the same. Because of the reduction in residual volume, total lung capacity is only slightly reduced. The reduction in residual volume has a minor impact on total lung capacity. The tidal volume is raised, resulting in an increase in minute volume [4]. Early in pregnancy, both renal plasma flow and glomerular filtration rate rise. The increase in glomerular filtration rate reaches 50%, lowering serum creatinine to 0.8 mg/dL, the upper limit of average. Only a few changes in the gastrointestinal tract during pregnancy are essential in terms of critical care. The time it takes for the stomach to clear and the chance of aspiration that comes with general anaesthesia are both increased during labour. Placental development may cause a significant increase in alkaline phosphatase, but this does not mean hepatic obstruction. Gallbladder stasis can lead to increased stone formation.
The liver is the primary source of net endogenous glucose development while not pregnant. Fasting glucose levels in pregnant women decline as the pregnancy progresses [5]. GDM is characterised as the presence of glucose concentrations in pregnant women that are at the upper end of the population range for glucose and are first observed during pregnancy [6]. Insulin sensitivity decreases overall during pregnancy. Maternal insulin sensitivity, characterised as a decrease in the glucose infusion rate during the euglycemic hyperinsulinemic clamp to maintain 90 mg/dL, decreases in lean women during early pregnancy [7]. Since lean women are more likely to begin their pregnancies with greater insulin sensitivity than obese women, the increases in insulin concentration are more pronounced in lean women [8]. During pregnancy, healthy pregnant women’s adipose tissue stores increase significantly. The mother and foetus can easily obtain calories from the subcutaneous stores, particularly during late pregnancy and lactation. Increases in visceral fat can be linked to decreased insulin sensitivity during late pregnancy [9].
In their research, Das and Sarka found that pregnant women faced a variety of difficulties when seeking health information, including inadequate hospital treatment, long wait times, anxiety and shame about discussing pregnancy with a physician, and a lack of time [10]. There are many discomforts that occur during pregnancy. Morning sickness, headache and backache, bladder and bowel changes, changes in hair and skin colour, indigestion and heartburn, leg cramps and swelling, vaginal thrush and discharge are the few common complications facing during pregnancy. As a result, the aim of this study was to describe the difficulties in obtaining health information and the measures to overcome the discomfort during pregnancy.
Research articles for this review were searched by using the keywords “pregnancy”, health issues”, “measures to overcome”, “challenges”. The following were used as exclusion criteria: 1) the subject was unrelated to the study’s goal; 2) there was no abstract available; 3) The research was limited to a single medical issue involving pregnancy in older women. 4) The report dealt with postpartum and maternity issues; and 5) the full research paper was not easily accessible. We looked for original research papers that were written in English and reported on studies that were performed using qualitative or quantitative methods. The current research did not include any other review papers. There were studies that looked at the health problems that women face during pregnancy were included in this review article.
According to previous literature, pregnant women’s dental health care demands differ dramatically from those of the general population. The most frequent oral health concerns during pregnancy include periodontal disease, Xerostomia, halitosis, and tooth movement. During pregnancy, the hormonal balance of pregnant women alters. Because the placenta produces increased levels of oestrogen and progesterone during pregnancy, several tissues endure modifications. Increased sensitivity to irritations arises in the gingiva during this time [11]. Low vitamin C levels are thought to be another cause of this condition. When compared to mothers with healthy periodontium, mothers with attachment loss have an increased risk of giving birth to babies with low birth weight [12]. Tooth decay is more common among pregnant women for a variety of reasons, including increased acidity in the mouth, sweet food demands, and a lack of attention to oral health. Vomiting can have a severe impact on oral hygiene and induce degradation of the mother enamel layer [13]. Due to the effect of pregnancy hormones, pregnant women bleed more easily and may postpone brushing their teeth and it leads to an increase in bacterial plaque [14]. Due to diminished flow of saliva, caries are more likely to develop at this time. Pregnancy oral tumour is indistinguishable from pyogenic granuloma and occurs in up to 5% of pregnancies. Increased progesterone, in combination with local irritants and microorganisms, causes this vascular lesion [15]. With a prevalence of 60 to 75 percent, gingivitis is the most frequent dental illness among pregnant women. A severe aggravation of preexisting gingivitis occurs in around half of all pregnant women [16]. Researchers discovered very few oral bacteria in the amniotic fluid and placenta of women who had preterm labour with periodontitis in one investigation [17]. PGE2 production reduces placental blood flow, resulting in placental necrosis and intrauterine growth restriction [18]. Salivary oestrogen levels are greater in women who are expecting preterm babies than in women who are expecting full-term babies. Salivary oestrogen promotes oral mucosa proliferation and desquamation, as well as a rise in subgingival crevicular fluid levels. Desquamating cells offer a favourable environment for bacterial growth by supplying nutrients, hence preventing infection [19].
Oral acid exposure is reduced through dietary and lifestyle changes, as well as the use of antiemetics, antacids, or both. Acid can be neutralised by rinsing the mouth with a teaspoon of baking soda in a cup of water after vomiting [20]. To lessen the risk of enamel damage, pregnant women should be encouraged to avoid brushing their teeth shortly after vomiting and to brush with a toothbrush with soft bristles when they do. Fluoride mouthwash can protect teeth that have been eroded or are sensitive. Proper dental hygiene can help women with previous periodontal disease lower the risk of recurrence or worsening disease during pregnancy. Education, clear communication, and the creation of continuing collaborative relationships can help physicians and dentists solve this dilemma. Physicians and dental colleagues can communicate information about the safety of dental treatment during pregnancy [21]. There is a link between plaque accumulation and caries prevalence during pregnancy and preventive maintenance methods. Mouthwashes or warm salty water should be gargled. Gums are relaxed and gum sensitivity is reduced by drinking warm salty water [22]. During this time, women can maintain their oral health by taking the required precautions, preventing potentially irreversible tooth disorders.
The mother’s cardiovascular physiology adapts significantly as a result of the hormonal changes that occur during pregnancy [23]. Oestrogen, progesterone, and relaxin levels rise early in the first trimester, resulting in systemic vasodilation [24]. The RAAS is activated to promote salt and water retention, resulting in an increase in plasma volume. When this is paired with an increase in ventricular wall mass, it results in greater stroke volume. During pregnancy, the combination of increased stroke volume and tachycardia causes an increase in cardiac output, which compensates for the decrease in vascular resistance in order to keep blood pressure high enough for mother and placental perfusion [25]. The increased volume load in the heart causes left ventricular hypertrophy, which is proportional to the increased cardiac labour necessary to accomplish the increased cardiac output [26]. Some changes in the systemic hemodynamics of pregnant women who are predisposed to hypertension may occur before the condition manifests itself clinically. A systolic blood pressure of 160 mmHg or a diastolic blood pressure of 110 mmHg, or both, indicates severe preeclampsia in pregnancy. Eclampsia is a severe form of pregnancy-induced hypertension that affects one in every 1,600 pregnancies and appears at the end of the pregnancy [27]. When compared to singleton pregnancies, twin pregnancies had more than three times the risk of developing hypertension during pregnancy [28]. Preeclamptic patients have lower renin levels than non-pregnant women, although they are still significantly higher than non-pregnant women. Because most preeclamptic individuals have a somewhat reduced plasma volume, maintaining relatively high levels of these hormones may be necessary [29].
Preeclampsia is the pathophysiology of de novo hypertension and proteinuria in pregnancy. The delivery of the placenta frequently triggers the remission of preeclampsia’s acute clinical symptoms, implying that the placenta plays a key role in the disease’s pathophysiology. The placenta undergoes substantial blood supply throughout normal pregnancy to allow circulation between the foetus and the mother [30]. The pathogenesis of preeclampsia has long been focused on altered uteroplacental blood flow. Relaxin is a hormone secreted more during pregnancy which acts as vasodilation. According to Jeyabalan et al., low first trimester relaxin concentrations were linked to an increased risk of preeclampsia [31].
For non-severe hypertension in pregnancy, oral labetalol is a first-line treatment [32]. Other beta-blockers, such as oxprenolol, are less thoroughly studied than labetalol, and it is used as a first-line treatment for non-severe hypertension in pregnancy [33]. In contrast, when oxprenolol was compared to methyldopa, the results and safety were found to be equal [34]. When mothers are exposed to calcium channel blockers during the first trimester, there is low teratogenicity [35]. Elsewhere in pregnancy, ACE inhibitors are still the first-line treatment for hypertension [36]. For non-severe hypertension, thiazide diuretics are considered second-line therapy.
The prevalence of gestational diabetes mellitus (GDM) is rising in lockstep with the rise in overweight and obesity among women of childbearing age. GDM-affected pregnancies increase the risk of caesarean and surgical vaginal delivery, macrosomia, neonatal hypoglycemia, and hyperbilirubinemia for both mother and child [37]. The onset of GDM is linked to a number of risk factors. Obesity, advanced maternal age, a significant family history of diabetes and belonging to an ethnic group are with a high prevalence of T2DM, polycystic ovarian syndrome, and chronic glucosuria. Because GDM usually starts in the late second trimester, when development is complete, congenital abnormalities do not occur at a higher rate in people with gestational diabetes. Because of the physiological, endocrine, and metabolic changes that occur throughout pregnancy in order to meet the fetus’s constant nutritional and oxygen needs, a diabetogenic condition comparable to type 2 diabetes (T2D) develops, increasing insulin resistance, lowering insulin sensitivity, and thus increasing the demand for insulin [38]. As a result of the increased placental glucose transport, maternal hyperglycemia causes foetal hyperinsulinemia. Foetal macrosomia is caused by a high insulin level in the foetus, which accelerates growth [39]. Although glucose metabolism changes during pregnancy, tolerance occurs and there is no effect on the mother or the foetus when insulin production rises. There is a higher risk of foetal when there is an inappropriate response. When the output of the pancreatic b-cells does not match the insulin requirement of the tissues as a result of alterations in insulin resistance, abnormal glucose tolerance ensues [40]. Early in pregnancy, fasting blood glucose levels drop, and this trend continues throughout the pregnancy. Insulin sensitivity decreases as pregnancy progresses, reaching pre-gravid levels about 34–36 weeks of pregnancy [40, 41]. Increases in hepatic glucose production during pregnancy show that the insulin action deficiency also affects the liver. Placental loss of anti-insulin hormones such as human placental lactogen, cortisol, oestrogen, and progesterone causes insulin resistance after mid-pregnancy. Low FBS, a low kidney glucose threshold, and enhanced insulin production are all effects of these hormones [42]. Maternal tissues become increasingly insulin resistant during pregnancy. This is thought to be produced in part by placental hormones and in part by unknown obesity and pregnancy-related variables. The main locations for glucose disposal throughout the body are skeletal muscle and adipose tissue. Insulin-mediated whole-body glucose elimination declines by 50% during pregnancy, and the woman must raise her insulin output by 200–250 percent to maintain a euglycemic condition [43]. Even while most women revert to a euglycaemic state immediately after delivery, women who have had GDM have a significantly higher chance of developing T2DM [44]. The biochemical relationship between GDM and T2DM is still unknown. Insulin resistance and/or aberrant insulin production define both illnesses [45]. Multiple potential protein indicators for later GDM have been discovered through proteomic screening in early pregnancy, including a cluster linked with insulin production, binding, resistance, and signalling [46]. An oral glucose tolerance test (OGTT) is usually used to identify GDM during 24–28 weeks of pregnancy. Because most of the physiologic insulin resistance of pregnancy will be firmly established, this timeframe has traditionally been favoured for routine GDM diagnosis. Another important difference in GDM testing techniques around the world is the ongoing debate over whether testing should be universal (for all pregnant women) or targeted solely for women with risk factors linked to a higher probability of a positive result.
Preventive interventions are needed to avoid the undesired consequences of obesity and hyperglycemia during pregnancy, given the global rise in obesity and the resulting increase in GDM [38, 47]. In roughly 70 to 85 percent of women with diagnosed GDM, lifestyle changes are enough to meet glycemic objectives [48]. Dietary counselling, in combination with physical activity and blood glucose self-monitoring, is the major intervention indicated for GDM [49]. A lower-carbohydrate diet with more animal protein and fat enhanced the risk of type 2 diabetes. As a result, it’s possible that the diet that’s best for treating GDM in women is not the best long-term diet [50]. Other nutritional treatments, such as probiotics and vitamin supplements, have gained popularity, but there is not enough data to suggest their widespread usage [51]. Insulin therapy is the preferred treatment because it does not cross the placenta and is thus deemed safe for the foetus. Metformin therapy was deemed safe and effective, and the women preferred it for insulin treatment [52]. Another study states that Metformin and sulfonylurea have been increasingly and safely used in the treatment of GDM [53]. In diabetic pregnant women with vitamin D deficiency/insufficiency, vitamin D administration can lower the chance of developing GDM and/or improve glycemic control [54]. Vitamin D regulates intracellular calcium to promote insulin production and attenuates insulin resistance by acting directly on pancreatic beta cells via the development of vitamin D receptors and the enzyme 25(OH)D-1-alfa-hydroxylase [55]. Furthermore, recent evidence from a large prospective trial suggests that increased physical activity may help reduce the risk of T2DM progression [56]. Exercise activities did not have a significant influence on the overall incidence of GDM in obese or overweight pregnant women, but when the effect measure was taken into account, the incidence of GDM was 24 percent lower in that group [57]. The following five components of guideline content were examined: GDM diagnosis, prenatal care, intrapartum care, neonatal care, and postpartum care. The majority of the suggestions in the guidelines were on prenatal care, particularly all types of therapy that could lower the risk of bad pregnancy outcomes due to uncontrolled blood sugar prior to conception [58]. The usage of information technology and digital platforms by diabetic pregnant women is fast rising around the world [59]. Telemedicine has been linked to high patient satisfaction since it allows for quick management of care across distances with fewer face-to-face physician appointments [60]. As a result, the use of e-platforms in the management of gestational diabetes shows encouraging results in terms of patient satisfaction and has no negative impact on pregnancy outcomes. Adequately powered RCTs are needed to assess whether such healthcare technologies are cost-effective or can help enhance care in urban or distant settings [61].
During pregnancy, several biological markers, particularly haematological, are physiologically altered. Biologists and doctors who are aware of these changes in the maternal body can screen for potential abnormalities. The haematological parameters must adjust in several ways, including providing vitamins and minerals for foetal haematopoiesis (iron, vitamin B12, folic acid), which can increase maternal anaemia, and preparing for birth bleeding, which is necessary to improve homeostasis [62]. The total blood volume increases by roughly 1.5 litres during pregnancy, primarily to meet the demands of the new vascular bed and to compensate for blood loss that occurs during birth [63]. At 6–12 weeks of pregnancy, the plasma volume expands by 10–15 percent. When maternal erythropoietin production rises, RBC mass rises as well, albeit at a slower rate than plasma volume, resulting in a drop in haemoglobin concentration. Dilutional anaemia is the result [64]. Haemodilution also contributes to a decrease in the rate of haematocrit (HCT) and haemoglobin (HGB), resulting in a false anaemia. Such a change is natural for pregnant women and demonstrates the adoption of a different threshold for the definition of pregnancy anaemia. The WHO defines anaemia in pregnancy as having a total circulating HGB concentration of less than 11 g/dl or an HCT of less than 33% at any point during the pregnancy. During pregnancy, RBC indices do not vary much. However, in an iron-replete woman, there is a slight rise in mean corpuscular volume (MCV) of around 4 fl, which peaks around 30–35 weeks gestation and does not indicate a vitamin B12 or folate shortage. The increased MCV can be explained by increased RBC production to fulfil the demands of pregnancy [65]. The haemoglobin concentration does not change until the 16th week of pregnancy, after which it falls steadily to the second trimester due to the expansion of plasma volume [66]. Haemodilution, or an increase in plasma volume greater than an increase in red cell mass, is the underlying cause of anaemia during pregnancy. This condition is also known as ‘physiological anaemia of pregnancy’ [67]. Because length is more stable than weight, haemoglobin demonstrated a positive connection with infant length but not with weight [68]. Haemoglobin and haematocrit increased on the first day after birth, decreased on the third and fifth days, and then began to rise again by day 42, achieving normal haemoglobin in non-pregnant women [69]. Because of the greater metabolic oxygen requirement, erythropoietin levels are 50 percent greater, which explains the mild bone marrow erythroid hyperplasia and enhanced reticulocyte count. A combination of a lowered maternal RBCs oxygen affinity from an enhanced 2,3 Diphosphoglycerate and a low maternal pCO2 results in enhanced oxygen transfer throughout the placenta [70].
Pregnancy causes an increase in white blood cell count, with the lowest limit of the reference range typically being 6,000/cumm. Leucocytosis occurs during pregnancy as a result of the physiologic stress that comes with being pregnant [71]. Throughout the first and second trimesters of pregnancy, lymphocyte count drops, then rises during the third trimester. Total leukocyte count levels rise significantly in the II and III trimesters, but there is no difference between pregnant and non-pregnant women in the I trimester. In the first trimester of pregnancy, non-anaemic women have a higher TLC count than anaemic women, but in the second and third trimesters, anaemic women have a higher TLC count than non-anaemic women [62]. During normal pregnancy, leukocytosis is caused by an enhanced inflammatory response, which can be caused by selective immunological tolerance, immunosuppression, and immunomodulation of the foetus [72]. During pregnancy, the ratio of monocytes to lymphocytes rises dramatically. During pregnancy, however, eosinophil and basophil numbers do not alter appreciably [73]. The neutrophil count starts to rise in the second month of pregnancy and reaches a plateau in the second or third trimester, when total white blood cell counts range from 9,000 to 15,000 cells per microliter.
In 7–8 percent of all pregnancies, gestational thrombocytopenia occurs. Due to rapid degradation, platelet counts are slightly lower which results in younger, bigger platelets present in pregnancy. The majority of thrombocytopenia in pregnancy is caused by increased blood loss [74]. Although the average platelet count falls monotonically during pregnancy, platelet aggregation increases, notably during the last 8 weeks of pregnancy [75]. The decline in the quantity of circulating platelets during pregnancy has been attributed to increased platelet consumption as well as a shorter life span in the uteroplacental circulation [76]. As the pregnancy progresses, the platelet volume distribution width widens dramatically and continually. As a result, as pregnancy progresses, the mean platelet volume becomes an insensitive indicator of platelet size.
Primary immune thrombocytopenia (ITP) affects about 3% of women who are thrombocytopenic at delivery. It occurs in 1/1000–1/10 000 pregnancies [77]. Two-thirds of women with ITP have pre-existing disease, according to most studies, and one-third are diagnosed for the first time during pregnancy [78]. The pathophysiological mechanism of thrombotic thrombocytopenic purpura (TTP) is thrombotic microangiopathy. Microangiopathic hemolytic anaemia, thrombocytopenia, fever, neurological signs, and renal impairment are all symptoms of TTP. Pregnancy is thought to be the trigger event in between 5 to 25% of TTP cases [79]. TTP occurs in the second trimester of pregnancy and occasionally in the postpartum period, although it is uncommon in the first trimester [80]. If TTP appears during the first trimester, regular plasma exchange may be able to maintain pregnancy.
Preventing anaemia in pregnancy requires effective communication about diet and nutrition to all pregnant women. Most experts recommend regular iron supplementation during pregnancy since the extra demand for iron is typically unmet by a typical diet. Although iron supplementation recommendations vary by location, the CDC recommends that all pregnant women begin a 30 mg/day iron supplementation [81]. he average iron density in a typical Indian diet is 8.5 mg/1000 Kcal, with 13.3 and 5.3 percent iron absorption in pregnancy from a rice-based and wheat-based Indian diet, respectively [82]. Women can use smartphone applications to learn about their daily iron needs, the iron content of various foods, and how to track their dietary iron intake. We support the creation and use of such applications. For improved absorption, all pregnant women should be told to take oral iron on an empty stomach or 1 hour after meals, preferably with a vitamin C-rich product like orange juice or guava. Supplement 2 outlines the oral iron treatments that can be used during pregnancy [82, 83].
The choice of therapy is based on the urgency of the platelet increase, the duration of the increase, and any potential side effects, and should be determined on an individual basis for each patient. Platelets should be available on standby if the mother’s platelet count remains low (50 109/l) around the time of delivery, but they are likely to be destroyed rapidly after infusion if due to an immune reaction, so they should be given in well-established rather than early labour if there are increased bleeding complications [84]. Given that there is no evidence that Caesarean delivery is safer for the foetus with thrombocytopenia than a simple vaginal delivery, which is usually safer than caesarean for the mother, the mode of delivery should be decided on obstetric concerns. Treatment may be required just during the later part of the third trimester to boost the platelet level before epidural anaesthesia or C section section if the individual is asymptomatic and the platelet count is more than 20*109/L [85]. Depending on the platelet level and stability, general measures such as avoiding aspirin, nonsteroidal anti-inflammatory medications, and intramuscular injections might be explored. Because low-dose aspirin is now commonly administered in pregnancy for a variety of reasons, it should not be avoided unless the risk of bleeding is significant. Prednisone at a low dose or intravenous immunoglobulin, or both, are viable alternatives in these circumstances. In symptomatic pregnant ITP patients or if the platelet count is less than standard level, other therapeutic options are available. When combined with intravenous immunoglobulin, a large dose of steroids can be employed [86]. Corticosteroids and intravenous IVIG are the most common treatments for maternal ITP [87].
When it came to getting health information, pregnant women faced personal, societal, and structural challenges. As a result, legislators and health planners should remove barriers, promote self-care, and improve the quality of life for pregnant women, ultimately improving their health. Pregnancy issues such as gestational diabetes mellitus, hypertension, preeclampsia, caesarean birth, and postpartum weight retention are all more likely in overweight and obese women. More research into the link between nutritional advancements and the rising prevalence of GDM in the developing world is needed. Iron supplementation has been linked to glucose dysregulation and hypertension in mid-pregnancy; its effectiveness and potential risks should be carefully considered.
I would like to thank Saveetha Institute of Medical and Technical Sciences for giving me this opportunity to carry out the research work.
No potential conflict of interest relevant to this article was reported.
This study received no specific support from public, private, or non-profit funding bodies.
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This topic will closely deal with all emerging trends in this discipline.",annualVolume:11411,isOpenForSubmission:!0,coverUrl:"https://cdn.intechopen.com/series_topics/covers/15.jpg",editor:{id:"441442",title:"Dr.",name:"Şükrü",middleName:null,surname:"Beydemir",fullName:"Şükrü Beydemir",profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0033Y00003GsUoIQAV/Profile_Picture_1634557147521",institutionString:null,institution:{name:"Anadolu University",institutionURL:null,country:{name:"Turkey"}}},editorTwo:{id:"13652",title:"Prof.",name:"Deniz",middleName:null,surname:"Ekinci",fullName:"Deniz Ekinci",profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0030O00002aYLT1QAO/Profile_Picture_1634557223079",institutionString:null,institution:{name:"Ondokuz Mayıs University",institutionURL:null,country:{name:"Turkey"}}},editorThree:null,editorialBoard:[{id:"241413",title:"Dr.",name:"Azhar",middleName:null,surname:"Rasul",fullName:"Azhar Rasul",profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0030O00002bRT1oQAG/Profile_Picture_1635251978933",institutionString:null,institution:{name:"Government College University, Faisalabad",institutionURL:null,country:{name:"Pakistan"}}},{id:"178316",title:"Ph.D.",name:"Sergey",middleName:null,surname:"Sedykh",fullName:"Sergey Sedykh",profilePictureURL:"https://mts.intechopen.com/storage/users/178316/images/system/178316.jfif",institutionString:null,institution:{name:"Novosibirsk State University",institutionURL:null,country:{name:"Russia"}}}]},{id:"17",title:"Metabolism",keywords:"Biomolecules Metabolism, Energy Metabolism, Metabolic Pathways, Key Metabolic Enzymes, Metabolic Adaptation",scope:"Metabolism is frequently defined in biochemistry textbooks as the overall process that allows living systems to acquire and use the free energy they need for their vital functions or the chemical processes that occur within a living organism to maintain life. Behind these definitions are hidden all the aspects of normal and pathological functioning of all processes that the topic ‘Metabolism’ will cover within the Biochemistry Series. Thus all studies on metabolism will be considered for publication.",annualVolume:11413,isOpenForSubmission:!0,coverUrl:"https://cdn.intechopen.com/series_topics/covers/17.jpg",editor:{id:"138626",title:"Dr.",name:"Yannis",middleName:null,surname:"Karamanos",fullName:"Yannis Karamanos",profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0030O00002g6Jv2QAE/Profile_Picture_1629356660984",institutionString:null,institution:{name:"Artois University",institutionURL:null,country:{name:"France"}}},editorTwo:null,editorThree:null,editorialBoard:[{id:"243049",title:"Dr.",name:"Anca",middleName:null,surname:"Pantea Stoian",fullName:"Anca Pantea Stoian",profilePictureURL:"https://mts.intechopen.com/storage/users/243049/images/system/243049.jpg",institutionString:null,institution:{name:"Carol Davila University of Medicine and Pharmacy",institutionURL:null,country:{name:"Romania"}}},{id:"203824",title:"Dr.",name:"Attilio",middleName:null,surname:"Rigotti",fullName:"Attilio Rigotti",profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",institutionString:null,institution:{name:"Pontifical Catholic University of Chile",institutionURL:null,country:{name:"Chile"}}},{id:"300470",title:"Dr.",name:"Yanfei (Jacob)",middleName:null,surname:"Qi",fullName:"Yanfei (Jacob) Qi",profilePictureURL:"https://mts.intechopen.com/storage/users/300470/images/system/300470.jpg",institutionString:null,institution:{name:"Centenary Institute of Cancer Medicine and Cell Biology",institutionURL:null,country:{name:"Australia"}}}]},{id:"18",title:"Proteomics",keywords:"Mono- and Two-Dimensional Gel Electrophoresis (1-and 2-DE), Liquid Chromatography (LC), Mass Spectrometry/Tandem Mass Spectrometry (MS; MS/MS), Proteins",scope:"With the recognition that the human genome cannot provide answers to the etiology of a disorder, changes in the proteins expressed by a genome became a focus in research. Thus proteomics, an area of research that detects all protein forms expressed in an organism, including splice isoforms and post-translational modifications, is more suitable than genomics for a comprehensive understanding of the biochemical processes that govern life. The most common proteomics applications are currently in the clinical field for the identification, in a variety of biological matrices, of biomarkers for diagnosis and therapeutic intervention of disorders. From the comparison of proteomic profiles of control and disease or different physiological states, which may emerge, changes in protein expression can provide new insights into the roles played by some proteins in human pathologies. Understanding how proteins function and interact with each other is another goal of proteomics that makes this approach even more intriguing. Specialized technology and expertise are required to assess the proteome of any biological sample. Currently, proteomics relies mainly on mass spectrometry (MS) combined with electrophoretic (1 or 2-DE-MS) and/or chromatographic techniques (LC-MS/MS). MS is an excellent tool that has gained popularity in proteomics because of its ability to gather a complex body of information such as cataloging protein expression, identifying protein modification sites, and defining protein interactions. The Proteomics topic aims to attract contributions on all aspects of MS-based proteomics that, by pushing the boundaries of MS capabilities, may address biological problems that have not been resolved yet.",annualVolume:11414,isOpenForSubmission:!0,coverUrl:"https://cdn.intechopen.com/series_topics/covers/18.jpg",editor:{id:"200689",title:"Prof.",name:"Paolo",middleName:null,surname:"Iadarola",fullName:"Paolo Iadarola",profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0030O00002bSCl8QAG/Profile_Picture_1623568118342",institutionString:null,institution:{name:"University of Pavia",institutionURL:null,country:{name:"Italy"}}},editorTwo:{id:"201414",title:"Dr.",name:"Simona",middleName:null,surname:"Viglio",fullName:"Simona Viglio",profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0030O00002bRKDHQA4/Profile_Picture_1630402531487",institutionString:null,institution:{name:"University of Pavia",institutionURL:null,country:{name:"Italy"}}},editorThree:null,editorialBoard:[{id:"72288",title:"Dr.",name:"Arli Aditya",middleName:null,surname:"Parikesit",fullName:"Arli Aditya Parikesit",profilePictureURL:"https://mts.intechopen.com/storage/users/72288/images/system/72288.jpg",institutionString:null,institution:{name:"Indonesia International Institute for Life Sciences",institutionURL:null,country:{name:"Indonesia"}}},{id:"40928",title:"Dr.",name:"Cesar",middleName:null,surname:"Lopez-Camarillo",fullName:"Cesar Lopez-Camarillo",profilePictureURL:"https://mts.intechopen.com/storage/users/40928/images/3884_n.png",institutionString:null,institution:{name:"Universidad Autónoma de la Ciudad de México",institutionURL:null,country:{name:"Mexico"}}},{id:"81926",title:"Dr.",name:"Shymaa",middleName:null,surname:"Enany",fullName:"Shymaa Enany",profilePictureURL:"https://mts.intechopen.com/storage/users/81926/images/system/81926.png",institutionString:"Suez Canal University",institution:{name:"Suez Canal University",institutionURL:null,country:{name:"Egypt"}}}]}]}},libraryRecommendation:{success:null,errors:{},institutions:[]},route:{name:"profile.detail",path:"/profiles/193439",hash:"",query:{},params:{id:"193439"},fullPath:"/profiles/193439",meta:{},from:{name:null,path:"/",hash:"",query:{},params:{},fullPath:"/",meta:{}}}},function(){var e;(e=document.currentScript||document.scripts[document.scripts.length-1]).parentNode.removeChild(e)}()