Examples of polypeptide sequences exhibiting affinity for various inorganics. (Reproduced from Nature Materials, 2003, volume 2, issue 9, 581. Copyright © 2003 Nature Publishing Group.)
\\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!
\\n"}]',published:!0,mainMedia:null},components:[{type:"htmlEditorComponent",content:'IntechOpen is proud to announce that 179 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 252 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!
\n'}],latestNews:[{slug:"stanford-university-identifies-top-2-scientists-over-1-000-are-intechopen-authors-and-editors-20210122",title:"Stanford University Identifies Top 2% Scientists, Over 1,000 are IntechOpen Authors and Editors"},{slug:"intechopen-authors-included-in-the-highly-cited-researchers-list-for-2020-20210121",title:"IntechOpen Authors Included in the Highly Cited Researchers List for 2020"},{slug:"intechopen-maintains-position-as-the-world-s-largest-oa-book-publisher-20201218",title:"IntechOpen Maintains Position as the World’s Largest OA Book Publisher"},{slug:"all-intechopen-books-available-on-perlego-20201215",title:"All IntechOpen Books Available on Perlego"},{slug:"oiv-awards-recognizes-intechopen-s-editors-20201127",title:"OIV Awards Recognizes IntechOpen's Editors"},{slug:"intechopen-joins-crossref-s-initiative-for-open-abstracts-i4oa-to-boost-the-discovery-of-research-20201005",title:"IntechOpen joins Crossref's Initiative for Open Abstracts (I4OA) to Boost the Discovery of Research"},{slug:"intechopen-hits-milestone-5-000-open-access-books-published-20200908",title:"IntechOpen hits milestone: 5,000 Open Access books published!"},{slug:"intechopen-books-hosted-on-the-mathworks-book-program-20200819",title:"IntechOpen Books Hosted on the MathWorks Book Program"}]},book:{item:{type:"book",id:"3116",leadTitle:null,fullTitle:"Advances in Industrial Design Engineering",title:"Advances in Industrial Design Engineering",subtitle:null,reviewType:"peer-reviewed",abstract:'A fast paced changing world requires dynamic methods and robust theories to enable designers to deal with the new product development landscape successfully and make a difference in an increasingly interconnected world. Designers continue stretching the boundaries of their discipline, and trail new paths in interdisciplinary domains, constantly moving the frontiers of their practice farther. \nThis book, the successor to "Industrial Design - New Frontiers" (2011), develops the concepts present in the previous book further, as well as reaching new areas of theory and practice in industrial design. "Advances in Industrial Design Engineering" assists readers in leaping forward in their own practice and in preparing new design research that is relevant and aligned with the current challenges of this fascinating field.',isbn:null,printIsbn:"978-953-51-1016-3",pdfIsbn:"978-953-51-6319-0",doi:"10.5772/3415",price:119,priceEur:129,priceUsd:155,slug:"advances-in-industrial-design-engineering",numberOfPages:252,isOpenForSubmission:!1,isInWos:1,hash:"9cb2d954a2f9ea36c3d0f915a7fcd8ad",bookSignature:"Denis A. 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Whizar-Lugo and Dr. José Ramón Saucillo-Osuna",publishedDate:null,coverURL:"https://cdn.intechopen.com/books/images_new/10708.jpg",keywords:"Regional Anesthesia, Ultrasound-Guided Regional Anesthesia, Local Anesthetics, Preventive Analgesia, Peripheral Blocks, Pediatric Regional Anesthesia, Intravenous Regional Anesthesia, Techniques, Complications, Adjuvants in Regional Anesthesia, Opioids, Alfa2 Agonists",numberOfDownloads:null,numberOfWosCitations:0,numberOfCrossrefCitations:null,numberOfDimensionsCitations:null,numberOfTotalCitations:null,isAvailableForWebshopOrdering:!0,dateEndFirstStepPublish:"February 23rd 2021",dateEndSecondStepPublish:"March 23rd 2021",dateEndThirdStepPublish:"May 22nd 2021",dateEndFourthStepPublish:"August 10th 2021",dateEndFifthStepPublish:"October 9th 2021",remainingDaysToSecondStep:"18 days",secondStepPassed:!1,currentStepOfPublishingProcess:2,editedByType:null,kuFlag:!1,biosketch:"Dr. Whizar-Lugo has published more than 100 publications on Anesthesia, Pain, Critical Care, and Internal Medicine. He works as an anesthesiologist at Lotus Med Group and belongs to the Institutos Nacionales de Salud as an associated researcher.",coeditorOneBiosketch:null,coeditorTwoBiosketch:null,coeditorThreeBiosketch:null,coeditorFourBiosketch:null,coeditorFiveBiosketch:null,editors:[{id:"169249",title:"Prof.",name:"Víctor M.",middleName:null,surname:"Whizar-Lugo",slug:"victor-m.-whizar-lugo",fullName:"Víctor M. Whizar-Lugo",profilePictureURL:"https://mts.intechopen.com/storage/users/169249/images/system/169249.jpg",biography:"Víctor M. Whizar-Lugo graduated from Universidad Nacional Autónoma de México and completed residencies in Internal Medicine at Hospital General de México and Anaesthesiology and Critical Care Medicine at Instituto Nacional de Ciencias Médicas y Nutrición Salvador Zubirán in México City. He also completed a fellowship at the Anesthesia Department, Pain Clinic at University of California, Los Angeles, USA. Currently, Dr. Whizar-Lugo works as anesthesiologist at Lotus Med Group, and belongs to the Institutos Nacionales de Salud as associated researcher. He has published many works on anesthesia, pain, internal medicine, and critical care, edited four books, and given countless conferences in congresses and meetings around the world. He has been a member of various editorial committees for anesthesiology journals, is past chief editor of the journal Anestesia en México, and is currently editor-in-chief of the Journal of Anesthesia and Critical Care. Dr. Whizar-Lugo is the founding director and current president of Anestesiología y Medicina del Dolor (www.anestesiologia-dolor.org), a free online medical education program.",institutionString:"Institutos Nacionales de Salud",position:null,outsideEditionCount:0,totalCites:0,totalAuthoredChapters:"5",totalChapterViews:"0",totalEditedBooks:"3",institution:null}],coeditorOne:{id:"345887",title:"Dr.",name:"José Ramón",middleName:null,surname:"Saucillo-Osuna",slug:"jose-ramon-saucillo-osuna",fullName:"José Ramón Saucillo-Osuna",profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0033Y000033rFXmQAM/Profile_Picture_1611740683590",biography:"Graduated from the Facultad de Medicina de la Universidad Autónoma de Guadalajara, he specialized in anesthesiology at the Centro Médico Nacional de Occidente in Guadalajara, México. He is one of the most important pioneers in Mexico in ultrasound-guided regional anesthesia. Dr. Saucillo-Osuna has lectured at multiple national and international congresses and is an adjunct professor at the Federación Mexicana de Colegios de Anestesiología, AC, former president of the Asociación Mexicana de Anestesia Regional, and active member of the Asociación Latinoamericana de Anestesia Regional.",institutionString:"Centro Médico Nacional de Occidente",position:null,outsideEditionCount:0,totalCites:0,totalAuthoredChapters:"0",totalChapterViews:"0",totalEditedBooks:"0",institution:null},coeditorTwo:null,coeditorThree:null,coeditorFour:null,coeditorFive:null,topics:[{id:"16",title:"Medicine",slug:"medicine"}],chapters:null,productType:{id:"1",title:"Edited Volume",chapterContentType:"chapter",authoredCaption:"Edited by"},personalPublishingAssistant:{id:"347258",firstName:"Marica",lastName:"Novakovic",middleName:null,title:"Dr.",imageUrl:"//cdnintech.com/web/frontend/www/assets/author.svg",email:"marica@intechopen.com",biography:null}},relatedBooks:[{type:"book",id:"6550",title:"Cohort Studies in Health Sciences",subtitle:null,isOpenForSubmission:!1,hash:"01df5aba4fff1a84b37a2fdafa809660",slug:"cohort-studies-in-health-sciences",bookSignature:"R. 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Venkateswarlu",coverURL:"https://cdn.intechopen.com/books/images_new/371.jpg",editedByType:"Edited by",editors:[{id:"58592",title:"Dr.",name:"Arun",surname:"Shanker",slug:"arun-shanker",fullName:"Arun Shanker"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}},{type:"book",id:"878",title:"Phytochemicals",subtitle:"A Global Perspective of Their Role in Nutrition and Health",isOpenForSubmission:!1,hash:"ec77671f63975ef2d16192897deb6835",slug:"phytochemicals-a-global-perspective-of-their-role-in-nutrition-and-health",bookSignature:"Venketeshwer Rao",coverURL:"https://cdn.intechopen.com/books/images_new/878.jpg",editedByType:"Edited by",editors:[{id:"82663",title:"Dr.",name:"Venketeshwer",surname:"Rao",slug:"venketeshwer-rao",fullName:"Venketeshwer Rao"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}},{type:"book",id:"4816",title:"Face Recognition",subtitle:null,isOpenForSubmission:!1,hash:"146063b5359146b7718ea86bad47c8eb",slug:"face_recognition",bookSignature:"Kresimir Delac and Mislav Grgic",coverURL:"https://cdn.intechopen.com/books/images_new/4816.jpg",editedByType:"Edited by",editors:[{id:"528",title:"Dr.",name:"Kresimir",surname:"Delac",slug:"kresimir-delac",fullName:"Kresimir Delac"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}}]},chapter:{item:{type:"chapter",id:"18167",title:"Bioinspired Synthesis of Organic/Inorganic Nanocomposite Materials Mediated by Biomolecules",doi:"10.5772/18411",slug:"bioinspired-synthesis-of-organic-inorganic-nanocomposite-materials-mediated-by-biomolecules",body:'\n\t\tMany organisms are capable of synthesizing organic/inorganic composites for protective or support purposes, such as bones, shells, and teeth. They exert a remarkable level of molecular control on particle size, structure, morphology, aggregation, and crystallographic orientation of these organic/inorganic structured materials. These materials often hierarchically arrange from nanoscale to macroscale (Feldheim and Eaton 2007; Dujardin and Mann 2002; Mann et al. 1993; Palmer et al. 2008; Estroff and Hamilton 2001; Aizenberg et al. 2005). For example, mollusks produce shells or nacres that contain a single distinct calcium carbonate crystalline phase, such as aragonite or calcite (Addadi et al. 2006). Magnetotactic bacteria produce Fe3O4 or Fe3S4 nanoparticles with well-defined sizes and shapes to recognize magnetic fields for alignment and migration (Dennis A. Bazylinski and Frankel 2004; Komeili 2007). Marine sponges produce silica spicules that have been demonstrated to possess light-guiding characteristics and may reach lengths of up to 3 m (Aizenberg et al. 2004; Sundar et al. 2003; Cattaneo-Vietti et al. 1996). In each of the examples listed above, and in many more examples in nature (Fig.1), specialized biomolecules, such as proteins, peptides, deoxyribonucleic acid (DNA), ribonucleic acid (RNA), and polysaccharides, have been found or are thought to play a critical role in directing the formation of these hierarchically assembled inorganic structures (Söllner et al. 2003; Müller et al. 2007). The participation of biomolecules in the nucleation and growth of crystals has attracted much research attention. Most notably, the proteins involved in directing the shape of these biomaterials have often evolved to recognize and bind selectively to one or more faces of the growing crystal. For instance, important matrix proteins involved in bone growth contain different function domains that orient the protein on hydroxyapatite nanocrystals and interact with target cell receptors (Gilbert et al. 2003). Nature has always been a source of inspiration for technical developments. Materials scientists consider the hierarchical structure of natural materials as a model for the development of new types of high-performance engineered materials (George and Ravindran 2010). The biomimetic approach could lead to the development of the controlled synthesis of inorganic nanophases, the crystal engineering of bulk solids, and the assembly of organized composite and ceramic materials (Mann et al. 1993).
\n\t\t\ta, Scanning electron microscopy (SEM) image of a growth edge of abalone (Haliotis rufescens) displaying aragonite platelets (blue) separated by organic film (orange) that eventually becomes nacre. (inset: transmission electron microscope (TEM) image). b, Magnetite nanoparticles formed by magnetotactic bacterium (Aquaspirillum magnetotacticum, inset: TEM image). c, Mouse enamel (SEM image) is a hard, wear-resistant material with highly ordered micro/nano architecture consisting of hydroxyapatite crystallites that assemble into woven rod structure (inset: schematic cross-section of a human tooth). d, SEM image of sponge spicule (with a cross-shaped apex shown in inset) has layered silica with excellent optical and mechanical properties. (Reproduced from Nature Materials, 2003, volume 2, issue 9, 578. Copyright © 2003 Nature Publishing Group.)
During the past decades, many inorganic crystals or hybrid inorganic/organic materials with special sizes, shapes, organization, complex forms, and hierarchies have been synthesized via bioinspired methods with the assistance of various templates, such as synthetic polymers, self-assembling peptides, proteins, and some low mass surfactant molecules (Cai and Yao 2010; Xu et al. 2007). Routine and reliable synthesis of self-assembled hybrid materials with tunable functionalities are urgently required for real-life applications and economic commercialization (Patil and Mann 2008; Gower 2008).
\n\t\t\tThere are mainly two mechanisms by which organisms control the self-assembled hierarchical organic/inorganic structures. First, the organic matrix serves as template on which to form a specific mineral. Second, inorganic materials usually appear in cells at the protoplasmic surface boundary layer. Therefore, the arrangement of the biominerals is controlled by the surface tension between the cells, the vesicles, and the growing mineral (Estroff and Hamilton 2001). Recent work in the field of bioinspired synthesis has achieved varying degrees of success in both of these strategies, especially the first mechanism, in which the self-assembling organic structures are used to template the growth of inorganic materials. The structural information from the organic assembly is directly transcribed to the inorganic materials, or used to modify the morphology of the inorganic phases.
\n\t\t\tThis review will focus on the recent successes in using self-assembling biomolecules as the organic matrix templates to direct and facilitate the formation of different kinds of structured organic/inorganic composite materials. The biomolecules are either natural or synthetic, including proteins, peptides, DNA, RNA, and polysaccharides.
\n\t\tThe use of biomolecules to direct the in vitro synthesis of inorganic materials is promising due to a number of reasons. The first of these potential benefits is the production of materials under mild reaction conditions (neutral pH, room temperature, aqueous solution etc.), while traditional methods require severe reaction conditions. The reduction of energy input and avoidance of harmful solvents makes bioinspired synthesis inherently “green” processing. The second major advantage of using biomolecules for materials synthesis is the elegant control on the size, shape, chemistry, and crystal structure of the inorganic product. These characteristics often impact or determine the properties of the synthesized material, making them have specific applications. Third, biomolecules offer the potential to produce materials with highly specific or multiple functions. Additionally, the large diversity of natural and synthetic biomolecules provides a high possibility of finding a biomolecule that can recognize, interact with, or direct the formation of an inorganic material (Dickerson et al. 2008).
\n\t\t\tThe primary sources to obtain the biomolecules used for the bioinspired synthesis of materials include: biomolecules isolated or derived from biomineralizing organisms, biomineralizing biomolecule analogs, and peptides identified for biomineralization (Dickerson et al. 2008). Biomolecules isolated or derived from biomineralizing organisms have been widely used for biomimetic synthesis of inorganic materials, however, the use of biomineral-isolated biomolecules has several drawbacks. For example, the biomolecules may be difficult to obtain or limited by the yield, may require specialized facilities to grow, and may provide few if any opportunities to modify or engineer protein sequences. Many of these difficulties may be overcome through the recombinant expression and subsequent purification of mineralizing proteins from bacterial cells (Tahir et al. 2005). Some of the sequence characteristics native to biomineralizing proteins may also be found in readily available and inexpensive proteins, such as hen egg white lysozyme (HEWL) or bovine serum albumin (BSA), making them popular candidates for biomimetic studies (Yang et al. 2006; Shiomi et al. 2007). According to these recognized sequences, biomineralizing biomolecule analogs can be developed. The analogs are not restricted to biomolecules, for instance, synthetic polymers are also developed as templates for bioinspired inorganic synthesis (Enlow et al. 2007; Kanapathipillai et al. 2008). The development of peptide, DNA, and RNA identification, separation, and synthesis techniques provides more opportunity to design templates for the bioinspired inorganic material synthesis, for example, phage display is used for identifying peptides and systematic enrichment of ligands by exponential enrichment (SELEX) is used for recognize RNA (Feldheim and Eaton 2007).
\n\t\t\tDifferent types of biomolecules used in bioinspired synthesis can be broadly categorized into four categories: proteins, peptides, nucleic acids, and polysaccharides. The role of these different types of biomolecules in the bioinspired synthesis and fabrication process is discussed in greater detail using specific cases as examples in the following sections.
\n\t\tProteins provide functional building blocks for the development of multi-functional materials (Gajjeraman et al. 2008). The self-assembly property of proteins would allow controlled organization of the organic/inorganic interface based on molecular recognition, resulting in hierarchical organization with desirable properties at multiple length scales. Proteins have superior specificity for target binding with complex molecular recognition mechanism (de la Rica and Matsui 2010). Through their unique and specific interactions with other macromolecules and inorganics, they process the ability to control structures and functions of biological hard and soft tissues in organisms (Sarikaya et al. 2003). In the following sections, several examples of protein-mediated bioinspired synthesis of structured organic/inorganic materials in vitro are highlighted.
\n\t\t\tBone is a highly ordered, dynamic, and highly vascularized tissue that exhibits excellent strength, hardness, and fracture toughness. It is a biocomposite of 70% mineral (mostly nanoscale calcium phosphate crystals) and 30% organics (including collagen, glycoproteins, proteoglycans, and sialoproteins) by dry weight (Salgado et al. 2004; Hu et al. 2010; Palmer et al. 2008). Calcium phosphates, notably HAp [Ca10(PO4)6(OH)2], exhibit many levels of hierarchical structures in bone from nano to macro scales (Rey et al. 2009). Mineralized collagen fibrils are the basic building block for bone formation. More than 20 human collagens have been reported. In collagens, the amino acids glycine, proline, and hydroxyproline account for more than 50% of the amino acid composition, often presented as the Gly-X-Y repeat unit (where X and Y are either proline or hydroxyproline) (Cui, et al. 2007). Most collagens display a 67 nm periodicity due to the axial packing of the individual collagen molecules (Prockop 1995). Collagens also serve as extracellular matrix molecules for many other soft and hard tissues, such as cartilage, tendons, and ligaments.
\n\t\t\t\tWe highlight some recent studies focused on the collagen-HAp interactions in the bioinspired synthesis of HAp composite materials. A nanocomposite of collagen and HAp was prepared in a continuous flow system, mimicking the situation in vivo, and resulted in a direct nucleation of HAp on the self-assembled collagen matrix. The biomineralization process of collagen and the self-organization mechanism were also analyzed. The inorganic crystals formed along the collagen fiber have similar a Ca-P ratio, crystalline degree, and carbonation extent to that observed in bone (Wang et al. 2006). Another study investigated the function of osteonectin in the formation of HAp. Osteonectin was added into the collagen solution, and results indicated that spindle-like nano-HAp could be deposited on collagen I/osteonectin and pure osteonectin (control) groups, but not on collagen II/osteonectin (Liao et al. 2009). This may help in understanding the biomineralization process in nature.
\n\t\t\t\tAnother collagen templated HAp nanocomposite showed equal or better biocompatibility than HAp ceramics, which was known to have excellent biocompatibility. The c-axes of HAp nanocrystals were regularly aligned along collagen fibrils, which was similar to natural bone orientation. The composite promoted the osteoclastic resorption, followed by new bone formation by osteoblasts, which was very similar to the reaction of a transplanted autogenous-bone. Therefore, the HAp/collagen composite can be potentially used as an artificial bone material in medical and dental fields (Kikuchi et al. 2004).
\n\t\t\t\tIn another study, two different bioinspired methods were used to fabricate HAp on collagen templates: dispersion of synthetic HAp in a solution of telopeptide-free collagen molecules and direct nucleation of HAp into reconstituted collagen fibers during their assembly. Composite materials obtained by direct nucleation showed similar composition, morphology, and structure to natural bone, and also indicated an intimated interaction between the inorganic phase and protein components (Tampieri et al. 2003). This proved the template function of the collagen during the bone formation.
\n\t\t\t\tProteins other than collagen are also used in bioinspired HAp synthesis. A novel human hair proteins and HAp composite was synthesized for using as a biomineral-scaffolding material. The human hair protein was soaked to a CaCl2 solution for fabrication into flat films. The flat films mainly consisted of α-keratin, which could bind 3 Ca2+ ions per 1 keratin molecule. The composite of the human hair protein and calcium phosphate was prepared via alternate soaking processes using CaCl2 and Na2HPO4 solutions. The diameters of deposited calcium phosphate particles were about 2–4 μm. The human hair proteins were not soluble and degraded during the soaking processes.(Fujii et al. 2009) Synthetic proteins have also been developed as templates for bioinspired synthesis. Self-assembled chimeric protein hydrogels comprising leucine zipper motifs flanking a dentin matrix protein 1 domain were developed to act as a HAp nucleator for the formation of highly oriented apatite similar to bone mineral (Gajjeraman et al. 2008).
\n\t\t\tMagnetotactic bacteria form magnetite nanoparticles in vivo with various morphologies (Bazylinski and Frankel 2004). The magnetospirillum magneticum strain AMB-1 produces a chain of cuboctahedral magnetite nanocrystals, each surrounded by a lipid bilayer membrane (Fig.1 b). Several proteins isolated from the magnetosome membranes showed common features in their amino acid sequences, which contain hydrophobic N-terminal and hydrophilic C-terminal regions. The C-terminal regions in Mms5, Mms6, Mms7, and Mms13 contain dense carboxyl and hydroxyl groups that bind ions. Nano sized magnetic particles similar to those in magnetotactic bacteria were prepared in vitro by chemical synthesis of magnetite in the presence of the protein Mms6. These proteins may be directly involved in biological magnetite crystal formation in magnetic bacteria (Arakaki et al. 2003).
\n\t\t\t\tTEM images of magnetite nanoparticles obtained by co-precipitation of FeCl2 and FeCl3: A) without protein, B) with Mms6, C) with ferritin, D) with Lnc2, and E) with BSA. Scale bars: 200 nm.” at the beginning of this line. (Adapted from Advanced Functional Materials, volume 17, issue 6, 952. Copyright © 2007 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.)
Similar in vitro synthesis of magnetite mediated by Mms6 was also achieved by other research groups. Recombinant Mms6 facilitated the formation of magnetite nanocrystals with uniform size (about 30 nm) in aqueous solution, which was verified by using TEM analysis and magnetization measurements. A polymeric gel was used to mimic the conditions at which magnetite nanocrystals were formed in magnetotactic bacteria and slow down the diffusion rates of the reagents. The nanocrystals formed in the presence of other proteins, as shown in Fig.2, did not exhibit the uniform sizes and shapes. Mms6-mediated magnetite nanoparticles demonstrated the largest magnetization values above the blocking temperature, and the largest magnetic susceptibility compared to those of the nanomaterials synthesized with other proteins. This study confirmed the hypothesis that Mms6 promotes the shape-selective formation of uniform superparamagnetic nanocrystals (T. \n\t\t\t\t\t\tProzorov et al. 2007\n\t\t\t\t\t).
\n\t\t\t\tSome inorganic magnetic materials which do not appear in living organisms, for example, cobalt ferrite (CoFe2O4) nanoparticles, were also synthesized in vitro by using Mms6 protein as a template. The recombinant full-length Mms6 protein or a synthetic C-terminal domain of Mms6 protein was covalently attached to self-assembling polymers (Pluronic F127) in order to template hierarchical growth of CoFe2O4 nanostructures, as shown in Fig.3. This new synthesis route enabled facile room-temperature shape-specific synthesis of complex magnetic crystalline nanomaterials with particle sizes of 40–100 nm, which were difficult to produce using conventional techniques (Tanya \n\t\t\t\t\t\tProzorov et al. 2007\n\t\t\t\t\t).
\n\t\t\t\tLeft, scheme for the protein-templated synthesis of CoFe2O4 nanocrystals in the presence of the Pluronic-conjugated recombinant Mms6 (red and blue colors stand for the Pluronic, and grey color stands for the protein); right, TEM of CoFe2O4 nanocrystals obtainedin the presence of Pluronic-conjugated c25-mms6. (Inset) High-resolution TEM image of a fragment of the central particle. (Reproduced from ACS Nano, volume 1, issue 3, 231. Copy right © 2007, American Chemistry Society.)
Aizenberg et al. reported the structural hierarchy of biosilica observed in the hexactinellid sponge Euplectella sp. (see Fig.4). The hierarchical structure overcomes the brittleness of its constituent material and shows outstanding mechanical rigidity and stability (Aizenberg et al. 2005).
\n\t\t\t\tStructural analysis of the mineralized skeletal system of Euplectella sp. (A) Photograph of the entire skeleton, showing cylindrical glass cage. (B) Fragment of the cage structure showing the square-grid lattice of vertical and horizontal struts with diagonal elements arranged in a chessboard manner. (C) SEM of a fractured and partially HF-etched single beam revealing its ceramic fiber-composite structure. (D) SEM of a cross section through a typical spicule in a strut, showing its characteristic laminated architecture. (E) Bleaching of biosilica surface revealing its consolidated nanoparticulate nature. (Adapted from Science, volume 309, issue 5732, 276. Copyright © 2005, American Association for the Advancement of Science.)
Silicateins, or silica proteins, were found to be enzymes (structural and catalytic proteins) that promote biosilica formation in nature (\n\t\t\t\t\t\tWang et al. 2010\n\t\t\t\t\t). The silicateins exhibit catalytic activity at neutral pH and low temperature. They have also been used as templates to direct the growth of silica particles along the axial protein filament. It has been used to simultaneously catalyze and structurally direct the hydrolysis and condensation of tetraethyl orthosilicate in vitro to form silica (Brutchey and Morse 2008). Silicatein filaments also demonstrated the ability to form titanium dioxide, gallium oxohydroxide (GaOOH) and gamma-gallium oxide (gamma-Ga2O3) in vitro, which are three inorganic semiconductors that biological species have never naturally produced (Kröger et al. 2006; Sumerel et al. 2003; Curnow et al. 2005; Kisailus et al. 2006). An enzymatic biocatalyst from the marine sponge Tethya aurantia, was used to catalyze and template the hydrolysis and condensation of the molecular precursor BaTiF6 at low temperature to form nanocrystalline BaTiOF4 (Brutchey et al. 2006).
\n\t\t\t\tAmorphous silica (or silica glass) is widely used in different applications, such as membranes, columns, heat-proof materials, optical communication fibers, and catalysts in organic synthesis (Jensen et al. 2009). Silicatein from the freshwater sponge Cauxi catalyzed the polymerization of this type of silica in vitro. Briefly, the sponge shot the axial protein filament in the desired growth direction, and then silicatein polymerized a thin silica layer around the filament. However, this silica deposition inhibited the transport of the siliceous acid to the axial filament, and a new set of silicatein were shot onto the newly synthesized silica deposition. This shooting process continued until the final diameter of spicules was reached. The process is shown by Fig.5. This study offered a new route for the development of mesoporous, amorphous silica with high purity under ambient condition (Jensen et al. 2009).
\n\t\t\t\tSchematic illustration of the growth mechanism of amorphous silica. (Reproduced from Journal of the Amrican Chemical Society, volume 131, issue 7, 2720. Copy right © 2009, American Chemistry Society.)
Silicateins could be immobilized onto a template surface, while still preserving their catalytic activity. In a bioinspired approach, biosilica was synthesized on “inert” surfaces (matrices) from monomeric precursors (Tahir et al. 2004). The matrices were first functionalized with a reactive polymer that was subsequently able to chemisorb nitrilotriacetic acid (NTA), a required binder for His-tagged recombinant silicatein. Silicatein that had been immobilized onto this matrix using NTA-His tag linkage had the capability to synthesize nanoparticulate biosilica, biotitania, and biozirconia from monomeric precursors. The process is shown by Fig.6.
\n\t\t\t\tThe biomimetic approach: The template (A) is successively functionalized with a reactive ester polymer (B) and the NTA linker (C). (D) Recombinant silicatein is bound via His-tag and Ni2+ to the NTA-polymer and subsequently mediates formation and assembly of polysilica formation (E). (Adapted from Applied Microbiology and Biotechnology, volume 83, number 3, 408. Copyright © 2009, Springer-Verlag.)
Fungi have been used in bioinspired synthesis of inorganic materials. Silica, zirconia, and titania nanoparticles were produced by mixing the fungus Fusarium oxysporum with aqueous anionic complexes SiF6\n\t\t\t\t\t2-, ZrF6\n\t\t\t\t\t2−, and TiF6\n\t\t\t\t\t2-, respectively. It has been shown that the extra-cellular protein of the Fusarium oxysporum mediated hydrolysis of the anionic complexes. These studies introduced a facile room temperature synthesis of crystalline titania and zirconia particles, whereas calcination at 300 ºC is required for crystallization of silica (Bansal et al. 2005; Bansal et al. 2004).
\n\t\t\tPeptides consist of short amino acid sequences that have less intricate functionality than proteins. Although peptides may not perform highly specialized functions compared to proteins, they can be synthesized more easily with desired amino acid sequences by well-established chemical and genetic engineering techniques. Therefore, they are widely used in the applications ranging from controlled gene and drug release, nanofabrication, biomineralization, and membrane protein stabilization to three-dimensional (3D) cell culture and tissue engineering. Peptides are designed to be folded in desired conformations, such as α-helix, β-sheet, etc. These 3D building blocks may yield supramolecular structures through self-assembly process. Moreover, the supramolecular structures can be controlled by changing the physicochemical properties of the environment such as pH, temperature, and salt content, which makes peptides versatile smart materials for the design of structured materials (de la Rica and Matsui 2010; Zhao et al. 2010).
\n\t\t\tThere are several possible ways of obtaining polypeptide sequences with specific affinity to inorganics. For example, well-established in vivo combinatorial biology protocols, phage display, and cell-surface display have been used to identify biological ligands and to map the molecular recognition site of antibodies. Table 1 shows the specific binding affinity of peptides for various inorganic materials.
\n\t\t\tA 12-residue peptide (NPYHPTIPQSVH-GGGK-biotin: CLP12 peptide) has been identified for HAp biomineralization using phage display. The sequence responsible for the mineralizing activity resembled the tripeptide repeat (Gly-Pro-Hyp) of type I collagen. This peptide was capable of binding to single crystal HAp and templating the nucleation and growth of crystalline HAp mineral in a sequence- and composition-dependent manner. (Chung et al.). In another study, polylysine and polyleucine based block copolypeptides (K170L30) were found to form gels at very low concentrations in aqueous media. The block copolypeptides have been used as templates for forming self-assembled calcium phosphate nanocomposites. The synthesis method allowed for simultaneous formation of the self-assembled block copolypeptide gel and of the inorganic phase. The inorganic contents accounted for over 50 wt% in the nanocomposite, approaching the inorganic content in bone (Hu et al. 2009). Thermoreversibly gelling block copolymers (Pluronic F127) conjugated to hydroxyapatite-nucleating peptides (DSKSDSSKSESDSS) were used to template the growth of inorganic calcium phosphate in aqueous solutions. The inorganic phase in the organic/inorganic nanocomposite was confirmed to be HAp. This work offered a route for the development of novel, self-assembling, injectable nanocomposite biomaterials for potential orthopedic applications (Yusufoglu et al. 2008).
\n\t\t\tSelf-assembling peptide amphiphiles have great potential as templates for nanofabrication. In 2001, a lipopeptide was designed and synthesized for biomineralization by the Stupp group (Hartgerink et al. 2001). In Fig.7 a and b, the C16 tail was connected to the N terminal of a peptide sequence which contained four cysteines, three glycines, a single phosphorylated serine and a cell adhesion ligand RGD (C16–C4G3S(p)RGD–OH). The C16 tail was hydrophobic and the peptide sequences were hydrophilic. These peptide amphiphlies self-assembled into cylindrical micellar structures in aqueous phase. C16 acyl tails packed themselves in the center of the micelle, while the peptide sequences formed β-sheets at the outside. There were disulfide bonds that formed by cross-linking of the four cysteine residues in the middle of the molecules, making the self-assembled nanofibers robust and impervious to pH variation (Fig.7 c). The nanofibers were then used to direct the
\n\t\t\t\n\t\t\t\t\t\t\tMaterials\n\t\t\t\t\t\t | \n\t\t\t\t\t\t\n\t\t\t\t\t\t\tSequences\n\t\t\t\t\t\t | \n\t\t\t\t\t\t\n\t\t\t\t\t\t\tSize\n\t\t\t\t\t\t | \n\t\t\t\t\t\t\n\t\t\t\t\t\t\tpI\n\t\t\t\t\t\t | \n\t\t\t\t\t\t\n\t\t\t\t\t\t\tMW\n\t\t\t\t\t\t | \n\t\t\t\t\t\t\n\t\t\t\t\t\t\tCharge\n\t\t\t\t\t\t | \n\t\t\t\t\t
\n\t\t\t\t\t\t | \n\t\t\t\t\t\t | \n\t\t\t\t\t\t | \n\t\t\t\t\t\t | \n\t\t\t\t\t\t | \n\t\t\t\t\t |
\n\t\t\t\t\t\t | MHGKTQATSGTIQS | \n\t\t\t\t\t\t14 | \n\t\t\t\t\t\t8.52 | \n\t\t\t\t\t\t1446.60 | \n\t\t\t\t\t\t+1 | \n\t\t\t\t\t
\n\t\t\t\t\t\t\tAu\n\t\t\t\t\t\t | \n\t\t\t\t\t\tSKTSLGQSGASLQGSEKLTNG | \n\t\t\t\t\t\t21 | \n\t\t\t\t\t\t8.31 | \n\t\t\t\t\t\t2050.12 | \n\t\t\t\t\t\t+1 | \n\t\t\t\t\t
\n\t\t\t\t\t\t | QATSEKLVRGMEGASLHPAKT | \n\t\t\t\t\t\t21 | \n\t\t\t\t\t\t8.60 | \n\t\t\t\t\t\t2211.52 | \n\t\t\t\t\t\t+1 | \n\t\t\t\t\t
\n\t\t\t\t\t\t | \n\t\t\t\t\t\t | \n\t\t\t\t\t\t | \n\t\t\t\t\t\t | \n\t\t\t\t\t\t | \n\t\t\t\t\t |
\n\t\t\t\t\t\t | DRTSTWR | \n\t\t\t\t\t\t7 | \n\t\t\t\t\t\t9.60 | \n\t\t\t\t\t\t920.98 | \n\t\t\t\t\t\t+1 | \n\t\t\t\t\t
\n\t\t\t\t\t\t\tPt\n\t\t\t\t\t\t | \n\t\t\t\t\t\tQSVTSTK | \n\t\t\t\t\t\t7 | \n\t\t\t\t\t\t8.75 | \n\t\t\t\t\t\t749.82 | \n\t\t\t\t\t\t+1 | \n\t\t\t\t\t
\n\t\t\t\t\t\t | SSSHLNK | \n\t\t\t\t\t\t7 | \n\t\t\t\t\t\t8.49 | \n\t\t\t\t\t\t771.83 | \n\t\t\t\t\t\t+1 | \n\t\t\t\t\t
\n\t\t\t\t\t\t | \n\t\t\t\t\t\t | \n\t\t\t\t\t\t | \n\t\t\t\t\t\t | \n\t\t\t\t\t\t | \n\t\t\t\t\t |
\n\t\t\t\t\t\t | SVTQNKY | \n\t\t\t\t\t\t7 | \n\t\t\t\t\t\t8.31 | \n\t\t\t\t\t\t838.92 | \n\t\t\t\t\t\t+1 | \n\t\t\t\t\t
\n\t\t\t\t\t\t\tPd\n\t\t\t\t\t\t | \n\t\t\t\t\t\tSPHPGPY | \n\t\t\t\t\t\t7 | \n\t\t\t\t\t\t6.46 | \n\t\t\t\t\t\t753.81 | \n\t\t\t\t\t\t0 | \n\t\t\t\t\t
\n\t\t\t\t\t\t | HAPTPML | \n\t\t\t\t\t\t7 | \n\t\t\t\t\t\t6.74 | \n\t\t\t\t\t\t765.93 | \n\t\t\t\t\t\t0 | \n\t\t\t\t\t
\n\t\t\t\t\t\t | \n\t\t\t\t\t\t | \n\t\t\t\t\t\t | \n\t\t\t\t\t\t | \n\t\t\t\t\t\t | \n\t\t\t\t\t |
\n\t\t\t\t\t\t | AYSSGAPPMPPF | \n\t\t\t\t\t\t12 | \n\t\t\t\t\t\t5.57 | \n\t\t\t\t\t\t1221.39 | \n\t\t\t\t\t\t0 | \n\t\t\t\t\t
\n\t\t\t\t\t\t\tAg\n\t\t\t\t\t\t | \n\t\t\t\t\t\tNPSSLFRYLPSD | \n\t\t\t\t\t\t12 | \n\t\t\t\t\t\t6.09 | \n\t\t\t\t\t\t1395.53 | \n\t\t\t\t\t\t0 | \n\t\t\t\t\t
\n\t\t\t\t\t\t | SLATQPPRTPPV | \n\t\t\t\t\t\t12 | \n\t\t\t\t\t\t9.47 | \n\t\t\t\t\t\t1263.46 | \n\t\t\t\t\t\t+1 | \n\t\t\t\t\t
\n\t\t\t\t\t\t | \n\t\t\t\t\t\t | \n\t\t\t\t\t\t | \n\t\t\t\t\t\t | \n\t\t\t\t\t\t | \n\t\t\t\t\t |
\n\t\t\t\t\t\t | MSPHPHPRHHHT | \n\t\t\t\t\t\t12 | \n\t\t\t\t\t\t9.59 | \n\t\t\t\t\t\t1470.63 | \n\t\t\t\t\t\t+1 | \n\t\t\t\t\t
\n\t\t\t\t\t\t\tSiO2\n\t\t\t\t\t\t | \n\t\t\t\t\t\tRGRRRRLSCRLL | \n\t\t\t\t\t\t12 | \n\t\t\t\t\t\t12.30 | \n\t\t\t\t\t\t1541.89 | \n\t\t\t\t\t\t+6 | \n\t\t\t\t\t
\n\t\t\t\t\t\t | KPSHHHHHTGAN | \n\t\t\t\t\t\t12 | \n\t\t\t\t\t\t8.87 | \n\t\t\t\t\t\t1359.43 | \n\t\t\t\t\t\t+1 | \n\t\t\t\t\t
\n\t\t\t\t\t\t | \n\t\t\t\t\t\t | \n\t\t\t\t\t\t | \n\t\t\t\t\t\t | \n\t\t\t\t\t\t | \n\t\t\t\t\t |
\n\t\t\t\t\t\t | VKTQATSREEPPRLPSKHRPG | \n\t\t\t\t\t\t21 | \n\t\t\t\t\t\t10.93 | \n\t\t\t\t\t\t2371.68 | \n\t\t\t\t\t\t+3 | \n\t\t\t\t\t
\n\t\t\t\t\t\t\tZeolites\n\t\t\t\t\t\t | \n\t\t\t\t\t\tMDHGKYRQKQATPG | \n\t\t\t\t\t\t14 | \n\t\t\t\t\t\t9.70 | \n\t\t\t\t\t\t1616.82 | \n\t\t\t\t\t\t+2 | \n\t\t\t\t\t
\n\t\t\t\t\t\t | \n\t\t\t\t\t\t | \n\t\t\t\t\t\t | \n\t\t\t\t\t\t | \n\t\t\t\t\t\t | \n\t\t\t\t\t |
\n\t\t\t\t\t\t | NTRMTARQHRSANHKSTQRA | \n\t\t\t\t\t\t20 | \n\t\t\t\t\t\t12.49 | \n\t\t\t\t\t\t2351.59 | \n\t\t\t\t\t\t+4 | \n\t\t\t\t\t
\n\t\t\t\t\t\t\tZnO\n\t\t\t\t\t\t | \n\t\t\t\t\t\tYDSRSMRPH | \n\t\t\t\t\t\t9 | \n\t\t\t\t\t\t8.75 | \n\t\t\t\t\t\t1148.26 | \n\t\t\t\t\t\t+1 | \n\t\t\t\t\t
\n\t\t\t\t\t\t | \n\t\t\t\t\t\t | \n\t\t\t\t\t\t | \n\t\t\t\t\t\t | \n\t\t\t\t\t\t | \n\t\t\t\t\t |
\n\t\t\t\t\t\t | HTQNMRMYEPWF | \n\t\t\t\t\t\t12 | \n\t\t\t\t\t\t6.75 | \n\t\t\t\t\t\t1639.87 | \n\t\t\t\t\t\t0 | \n\t\t\t\t\t
\n\t\t\t\t\t\t\tCaCO3\n\t\t\t\t\t\t | \n\t\t\t\t\t\tDVFSSFNLKHMR | \n\t\t\t\t\t\t12 | \n\t\t\t\t\t\t8.75 | \n\t\t\t\t\t\t1480.90 | \n\t\t\t\t\t\t+1 | \n\t\t\t\t\t
\n\t\t\t\t\t\t | \n\t\t\t\t\t\t | \n\t\t\t\t\t\t | \n\t\t\t\t\t\t | \n\t\t\t\t\t\t | \n\t\t\t\t\t |
\n\t\t\t\t\t\t | VVRPKAATN | \n\t\t\t\t\t\t9 | \n\t\t\t\t\t\t11.00 | \n\t\t\t\t\t\t955.13 | \n\t\t\t\t\t\t+2 | \n\t\t\t\t\t
\n\t\t\t\t\t\t\tCr2O3\n\t\t\t\t\t\t | \n\t\t\t\t\t\tRIRHRLVGQ | \n\t\t\t\t\t\t9 | \n\t\t\t\t\t\t12.30 | \n\t\t\t\t\t\t1134.35 | \n\t\t\t\t\t\t+3 | \n\t\t\t\t\t
\n\t\t\t\t\t\t | \n\t\t\t\t\t\t | \n\t\t\t\t\t\t | \n\t\t\t\t\t\t | \n\t\t\t\t\t\t | \n\t\t\t\t\t |
\n\t\t\t\t\t\t\tFe2O3\n\t\t\t\t\t\t | \n\t\t\t\t\t\tRRTVKHHVN | \n\t\t\t\t\t\t9 | \n\t\t\t\t\t\t12.01 | \n\t\t\t\t\t\t1146.32 | \n\t\t\t\t\t\t+3 | \n\t\t\t\t\t
\n\t\t\t\t\t\t | \n\t\t\t\t\t\t | \n\t\t\t\t\t\t | \n\t\t\t\t\t\t | \n\t\t\t\t\t\t | \n\t\t\t\t\t |
\n\t\t\t\t\t\t | AQNPSDNNTHTH | \n\t\t\t\t\t\t12 | \n\t\t\t\t\t\t5.97 | \n\t\t\t\t\t\t1335.31 | \n\t\t\t\t\t\t0 | \n\t\t\t\t\t
\n\t\t\t\t\t\t\tGaAs\n\t\t\t\t\t\t | \n\t\t\t\t\t\tRLELAIPLQGSG | \n\t\t\t\t\t\t12 | \n\t\t\t\t\t\t6.00 | \n\t\t\t\t\t\t1253.46 | \n\t\t\t\t\t\t0 | \n\t\t\t\t\t
\n\t\t\t\t\t\t | TPPRPIQYNHTS | \n\t\t\t\t\t\t12 | \n\t\t\t\t\t\t8.44 | \n\t\t\t\t\t\t1410.55 | \n\t\t\t\t\t\t+1 | \n\t\t\t\t\t
\n\t\t\t\t\t\t | \n\t\t\t\t\t\t | \n\t\t\t\t\t\t | \n\t\t\t\t\t\t | \n\t\t\t\t\t\t | \n\t\t\t\t\t |
\n\t\t\t\t\t\t\tZnS\n\t\t\t\t\t\t | \n\t\t\t\t\t\tNNPMHQN | \n\t\t\t\t\t\t7 | \n\t\t\t\t\t\t6.74 | \n\t\t\t\t\t\t853.91 | \n\t\t\t\t\t\t0 | \n\t\t\t\t\t
Examples of polypeptide sequences exhibiting affinity for various inorganics. (Reproduced from Nature Materials, 2003, volume 2, issue 9, 581. Copyright © 2003 Nature Publishing Group.)
a) Chemical structure of the peptide amphiphiles. (b) Molecular model of the peptide amphiphiles. (c) Schematic model of the self-assembly of peptide amphiphiles into a cylindrical micelle. (Reproduced from Chemical Reviews, volume 108, issue 11, 4776. Copyright © 2008, American Chemical Society.)
mineralization of HAp. The HAp nucleated on the surfaces of the lipopeptide nanofibers and its crystals grew with their c-axes oriented along the long axes of the nanofibers. This alignment was the same as that observed between collagen fibers and HAp crystals in bone (Hartgerink et al. 2001; Zhao et al. 2010).
\n\t\t\tShorter peptide I3K may form nanotubes with diameters about 10 nm and lengths over 5 mm. The nanostructure from this ultra-short peptide indicated that the amphiphilicity of a peptide amphiphile can be balanced between the length of a peptide sequence and the size of hydrophobic amino acids. I3K molecules were thought to initially interdigitate with each other through the hydrophobic interaction among the I3 tails, forming bilayer fragments. The self-assembly was driven by the hydrophobic affinity between isoleucine residues with the I3 tails packed in the middle and the K residues projected at the outside, facing the water. The peptide bilayer fragments then further assembled into twisted ribbons.
\n\t\t\tA schematic representation of I3K self-assembly process leading to the formation of peptide nanotubes which can then serve as templates for silicification. (Reproduced from Chemical Society Reviews, volume 39, issue 9, 3484. Copyright © Royal Society of Chemistry 2010.)
The fusion of the helical ribbons resulted in the formation of stable nanotubes, indicating the strong driving force along the main axial direction of the nanotubular structure. Fig.8 shows the self-assembling process. Because of their extreme stability against heating or exposure to organic solvents, I3K nanotubes were used as templates for silicification from the hydrolysis of TEOS (tetraethoxysilane) precusor. The lysine groups on the inner and outer nanotube surfaces catalyzed the silicification, leading to the formation of silica nanotubes (Xu et al. 2010).
\n\t\tDNA and RNA can self-assemble into well-defined secondary and tertiary structures at the nanoscale, which provide an ideal template for the formation of nanocrystals (Loweth et al. 1999). DNA templated gold nanoparticles have attracted much attention, as the self-assembled DNA nanostructures offer programmable scaffolds to organize the gold nanoparticles (Ding et al. 2010; Zhang et al. 2006; \n\t\t\t\t\tWang et al. 2010\n\t\t\t\t). A self-assembled two-dimensional (2D) DNA nanogrid was used as a template to grow 5-nm gold nanoparticles (Au NPs) into periodic square lattices, as shown by Fig. 9. The center-to-center distance between neighboring particles was about 38 nm. These accurate controlled Au NPs distribution may find applications in nanoelectronic and nanophotonic devices (Zhang et al. 2006).
\n\t\t\tUp left: the 2D DNA nanogrids with the single strand A15 out of the plane; up down: assembly of 5-nm Au NPs on the DNA grids. The zigzag black lines surrounding the Au NPs represent the T15 strands covalently linked to the surface of the particle through Au−S bonds. The right imagess are the AFM height data corresponding to each of their left. (Reproduced from Nano Letters, volume 6, issue 2, 248. Copyright © 2006, American Chemical Society.)
A chemically well-defined bio-core in an inorganic shell nanohybrid material was recently reported. It consisted of a DNA molecule as the bio-core with a size of 100 nm and a spherical inorganic nanoshell reassembled with exfoliated layered metal hydroxide (MH) with an overall thickness of 10 nm. The negatively charged DNA molecules can be encapsulated into a positively charged inorganic nanocavity of self-assembled MH nanosheets, as illustrated in Fig.10. Due to the pH-dependent solubility of the MH nanoshell, the DNA can be encapsulated and released, which play a crucial role in maximizing the stability of base sequence-manipulated and probe-functionalized DNA molecules with designed information. Therefore, these hybrid materials could be used as advanced gene delivery systems and a biomedical diagnostics system for DNA-based information (Park et al. 2010).
\n\t\t\tScheme, TEM and SEM image for the designed DNA@Inorganic Core−Shell nanohybrid. (Reproduced from Journal of the American Chemical Scociety, volume 132, issue 47, 16735. Copyright © 2010, American Chemical Society.)
A multi-lamellar structure was formed by complexes of anionic DNA and cationic liposomes self-assembly. The two-dimensional lipid sheets confined a periodic one-dimensional lattice of parallel DNA chains, as shown by Fig.11. These simple DNA-membrane templates could be used for controlled CdS crystalline synthesis. Cd2+ ions condensed on the DNA chains, and subsequently reacted with H2S to form CdS nanorods. Depending on the charge of the membrane, different concentrations of Cd2+ ions condense onto the template, and different morphologies of CdS were formed. The degree of template overcharging was determined by the relative stoichiometry of DNA and cationic membrane lipids (Liang et al. 2004).
\n\t\t\tSchematic representation of CdS growth within DNA-membrane complexes: the Cd2+ ions (red balls) are organized by DNA strands (blue) in the lamellar DNA−membrane complexes (side-view). (Reproduced from Journal of American Chemical Society, volume 126, issue 43, 14158. Copyright © 2004, American Chemical Society.)
One kind of DNA molecules were reported to mediate the nucleation and growth of the calcium carbonate particles. CaCO3 microspheres with different surface morphologies were prepared in the presence of the DNA, indicating that DNA could induce biomineralization in the biological system. It was found that the DNA concentration influenced on the surface structures of CaCO3 particles significantly. This research provided new insight into the morphological control of CaCO3 and other inorganic materials (Cheng et al. 2010).
\n\t\t\tThe Kelley group investigated the role of RNA secondary structure on the growth of CdS nanocrystals. They showed that a folded wild-type tRNA (wtRNA) and an unfolded mutant tRNA (mtRNA) of identical length were both able to mediate the formation of CdS during its spontaneous precipitation from solution, but they saw differences in the average nanocrystal sizes and size distributions. A narrow distribution around 6 nm diameter particles was found for particles grown with wtRNA, while mtRNA generated a bimodal distribution of 7 and 11.5 nm diameter particles. This is a good illustration that a biomolecule can affect the nanocrystal size (Ma, Dooley, and Kelley 2006).
\n\t\tA slow but increasing interest has been developing to explore the role of polysaccharides in biomineralization, despite the fact that they have been prevalent since the early stages of evolution. Single types of polysaccharides are typically not associated with biominerals. Only hydroxylated, carboxylated, or sulfated polysaccharides, or those containing a mixture of these functional moieties, are found in biominerals (Arias and Fernández 2008). Chitin is the second most abundant natural polymer after cellulose on earth. It is a linear polysaccharide of β-(1-4)-2-acetamido-2-deoxy-d-glucose. The chemical structure of chitin is very similar to that of cellulose, with a hydroxyl group replaced by an acetamido group. Pure chitin with 100% acetylation does not exist in nature. Chitin tends to form a co-polymer with its N-deacetylated derivative, chitosan. Chitosan is a polymer of β-(1-4)-2-amino-2-deoxy-d-glucose. The chemical structures of cellulose, chitin, and chitosan are shown in Fig.12 (Meyers et al. 2008).
\n\t\t\tChemical structures of chitin, chitosan, and cellulose.
Chitosan composite materials have attracted much research interest in bone tissue engineering due to their minimal foreign body reactions, intrinsic antibacterial nature, biocompatibility, biodegradability, and ability to be molded into various geometries and forms. Recently, grafted chitosan natural polymer with carbon nanotubes has been incorporated to increase the mechanical strength of artificial bone (Venkatesan and Kim 2010). Laminated HAp/chitosan nanocomposites and nano-HAp/chitosan-pectin composites were prepared and showed improved strength, especially in moist environments. This combination can be expanded to other HAp-biopolymer systems, thus offer a new insight for fabricating biomimetic nanocomposites (Li et al. 2010; Zuo et al. 2010).
\n\t\t\tChitosan was also used as organic template to form HAp nanocrystals. Spindle shaped HAp with 30- 40 nm length and 7- 8 nm width was synthesized through the biomimetic method with chitosan as template. The spindle shaped nano HAp grew in a 0.5wt% chitosan solution for 7 days. The crystallinity of samples increased with the aging time. The HAp powders synthesized with chitosan as templates had good thermal stability up to 800 °C (He et al. 2007).
\n\t\t\tDesign and synthesis of bacterial cellulose/HAp nanocomposites was reported for bone healing applications using a bioinspired approach. Bacterial cellulose with various surface morphologies (pellicles and tubes) was negatively charged by the adsorption of carboxymethyl cellulose to initiate nucleation of calcium-deficient hydroxyapatite (cdHAp). The cdHAp was grown in vitro via dynamic simulated body fluid treatments for 7 days (Zimmermann et al. 2011). Cellulose also used to template the growth of silica. Through in-situ growth of silica nanoparticles on cotton fabrics, a dual-scaled surface with nanoscaled roughness of silica and microscaled roughness of cellulose fiber was generated (Chen et al. 2010).
\n\t\tIn summary, in the recent past, there has been remarkable progress in the development of bioinspired procedures for controlling inorganic crystal nucleation and growth, especially at the nanoscale. Biomolecules have been successfully utilized to produce a variety of self-assembled structured inorganic materials under relatively mild conditions. Biomolecules have been found to be able to direct or modify the shapes, sizes, crystal structures, and other properties of the synthesized inorganic materials. Examples of such bioinspired inorganic nanostructures include HAp, SiO2, Fe3O4, CdS, TiO2, ZrO2, gold and silver etc., which have applications in biomedical, biosensor, bioceramic, and other fields. Modern biotechnology has also enabled the construction of chimeric biomolecules with desired properties, which may be utilized to create hierarchical assembled and reinforced composite materials.
\n\t\t\tIn the recent past, many biomolecules promoting materials synthesis have been identified. The number of inorganic materials that could be used for bioinspired synthesis has also been expanded. However, our fundamental understanding of these existing topics must be furthered in order to more fully harness the potential of biomolecules for material synthesis. There are also a number of interesting and powerful new concepts that have received only a little attention or remain unexplored. Design of more hierarchically self-assembled biomolecules that could template and direct the inorganic formation is also required. With the continued attention and ingenuity of researchers from diverse disciplines, the future of biomimetic materials synthesis promises to be exciting, dynamic, and rich in applications.
\n\t\tThis work was supported by the U.S. Department of Energy, Office of Basic Energy Science, Division of Materials Sciences and Engineering. The research was performed at the Ames Laboratory. Ames Laboratory is operated for the U.S. Department of Energy by Iowa State University under Contract No. DE-AC02-07CH11358.
\n\t\tLeiomyomas are benign smooth muscle tumours usually arise from the uterus [1]. Classical uterine leiomyoma manifest as firm, well circumscribed mass, and localized to the pelvic cavity [2]. Extrauterine leiomyomas (EULs) are very rare and their etiology is not clear [1]. They grow in unusual patterns and locations, thus possess greater diagnostic challenge. Different presentations of EUL are disseminated peritoneal leiomyomatosis (DPL), parasitic leiomyoma (PL), uterine-like mass lesions, adenomyoma and endomyometriosis [3]. Unusual sites involvement like vulval and rectovaginal leiomyomas are also found [4]. EULs arising in the gastrointestinal tract, genitourinary tract, as well as other rare locations including sinonasal cavities, orbits, and skin are also described in some case reports.
\nUterine leiomyoma is a benign tumour which originates from smooth muscle cells. Leiomyomas can present in abnormal growth patterns and tend to occur in extrauterine location especially in cases with prior history of hysterectomy or surgery for uterine leiomyomas.
\nMultifocal proliferation of multiple smooth nodules throughout the peritoneal surface histologically similar to uterine myomas is known as leiomyomatosis peritonealis disseminate (LPD) or disseminated peritoneal leiomyomatosis (DPL) [3, 5, 6]. The peritoneal cavity shows multiple nodules of smooth muscle (Figure 1) [6, 7]. DPL usually occurs in reproductive age group with an indolent course, and are mostly detected incidentally [6]. Uterine myoma morcellation is a known risk factor for the development of DPL with an incidence rate around 0.12 to 0.95% after morcellation [5, 6]. Morcellation may lead to spreading of cellular materials of the myoma fragments. These morcellated tissues get disseminated if they are not removed and may become infarcted, necrotic or even parasitic [3]. Other causes which can contribute in the pathogenesis of DPL includes; hormonal, genetic, and sub-peritoneal mesenchymal stem cells metaplasia.
\n(A) Contrast-enhanced T1-weighted fat-suppressed fast spin echo magnetic resonance image shows multiple homogeneously enhancing peritoneal leiomyomas (arrows), (B) Intra-operative gross image showing multiple variably sized peritoneal nodules representing disseminated peritoneal leiomyomatosis.
Pelvic region is the commonest site especially in pouch of douglas, may also spread to entire abdomen to involve omentum and mesentery. DPL is very invasive and very difficult for complete surgical excision, which may invade into bladder, retroperitoneal space, liver and small bowel [5]. They present as numerous subcentimetric grey -white firm nodules, sometimes with solid cystic hemorrhagic changes [5]. DPL can presents with ascites and adenopathy, which can be confused with peritoneal carcinomatosis. Sometimes, DPL may evolve into leiomyosarcoma, though it is extremely rare and possess high mortality rate [5, 6]. Due to unusual multifocal presentation, peritoneal myomas mimic malignant peritoneal tumor, so aggressive treatment at first surgical line should be avoided [6].
\nSome cases of gastrointestinal tract (GIT) leiomyomas have been reported with intestinal obstruction or bleeding without past or present history of uterine fibroid. But GIT leiomyomas are different from LPD. GIT leiomyomas can develop from intestinal wall and may reach the lumen whereas LPD mostly reach peritoneal cavity and omentum [5]. But disseminated GIT leiomyoma could be related to LPD, if there is no evidence of uterine myomas [5].
\nBenign metastasizing leiomyoma (BML) is a rare condition that affects women with a history of uterine myomectomy, which is found to metastasize to extra-uterine sites. The disease is characterized by monoclonal proliferation of smooth muscle cells and haematogenous spread from uterine leiomyoma to distant locations, most commonly the lungs (Figure 2) [2, 8]. The other uncommon site of metastasis includes heart and spinal cord [2]. Metaplastic transformation of the coelomic epithelium may explain BML in almost any place where mesothelial mesenchyme exists [2]. BML commonly occur during peri-menopausal period. Surgical excision is the treatment of choice.
\n(A) Abdomino-pelvic computed tomography showing a large pelvic mass, and (B) thoracic computed tomography showing bilateral lung nodules, Gross specimens (C) pelvic mass excision and (D) video-assisted thoracoscopic guided surgical resection of bilateral basal lung nodule in an operated case of total abdominal hysterectomy with bilateral salpingo-oopherectomy.
Intravenous leiomyomatosis (IVL) also included under smooth muscle tumours with unusual growth pattern like that of benign metastasizing leiomyoma (BML) and diffuse peritoneal leiomyomatosis (DPL) and difficult to distinguish from them [2]. IVL is very rare variant of benign leiomyomas. It presents as fragile and malleable leiomyoma that extends through adjacent venous structures in a worm-like fashion (Figure 3) [2]. Rarey, IVL may infiltrate into the right heart chamber and the lungs [6]. Due to wide range of clinical manifestation, IVL is difficult to diagnose pre-operatively [2].
\n(A) Magnetic resonance image showing a ‘comma’ shaped thrombosis, extending from the intrahepatic portion of inferior vena cava (IVC) to the right atrium, (B) Echocardiography showing an intracardiac mass with dynamic movement past the tricuspid valve into the right ventricle, (C) Gross specimen of total abdominal hysterectomy with left salpingo-oophorectomy, and IVC and intracardiac mass.
Parasitic leiomyoma is termed when leiomyoma especially subserous fibroid is pedunculated off the uterine serosa or when fragments of a fibroid detach, get implanted and grow within the peritoneal cavity or becomes adherent to other structures, especially the omentum (Figure 4) [3]. They obtain their blood supply from nearby organ and the uterine pedicle either or become avascular and disappear completely. These are also known as ectopic leiomyoma [3]. Cucinella et al. suggested morcellated hysterectomies or myomectomies as an important cause for development of parasitic leiomyoma [9].
\n(A) Magnetic resonance image showing two large lobulated peritoneal masses with similar signal and enhancement characteristics, (B) Gross specimen of peritoneal fibroid vascularized by omental vessels in a patient underwent laparoscopic myomectomy 5 years earlier.
Extrauterine adenomyomas (EUA) are benign tumours composed of smooth muscles, endometrial glands and endometrial stroma (Figure 5) [10]. In the literature, four hypotheses have been proposed for the development of EUA which includes (1) Müllerian duct fusion defect - the failure of fusion of Müllerian ducts result in either duplication or atresia of the uterus which is suggested by the formation of uterine-like masses, (2) Subcoelomic mesenchyme transformation - Subcoelomic mesenchyme is a layer of tissue that lies underneath the mesothelial surface of the peritoneum. It also lies underneath the subserosal stroma of uterus, uterine ligaments, ovaries and fallopian tubes, (3) Müllerianosis - It is a heterotopic Müllerian rests incorporated into other organs during organogenesis which may proliferate in response to hormones and (4) Endomyometriosis - along with endomyometriosis, smooth muscle hyperplasia or metaplasia leads to EUA [11, 12].
\nIntra-operative laparoscopic images of (A) pararectal adenomyoma and (B) right ovarian adenomyoma, histopathology images of ovarian adenomyoma (C) low power and (D) high power delineating smooth muscle bundles with embedded endometrial glands in a patient underwent laparoscopic myomectomy 5 years earlier.
Leiomyomas are clonal neoplasm and express more number of estrogen and progesterone receptors in comparison to normal myometrium [1, 2]. Circulating estrogen, progesterone and other growth factors like epidermal growth factor and insulin like growth factors are involved in the growth of uterine leiomyomas [1]. Estrogen stimulates the growth of leiomyoma independent of its location whether uterine or extrauterine [1]. However, the role of progesterone remains uncertain in extrauterine leiomyoma and it’s serum levels are either normal or low. Withdrawal of progesterone and of sex steroid down regulates expression of estrogen receptors (ER) in both leiomyomas and myometrium. This indicates that progesterone and progestins have a dual role on leiomyomas. First, limitation of the tissue response due to blocking of ER replacement and leading to unopposed estrogenic growth effect either by direct stimulation or by increased expression of progesterone receptors (PR). Second, progesterone may leads to an intrinsic growth-stimulation [1]. Progesterone causes increased mitotic division causing myoma growth and leads to the higher propensity for development of the somatic mutations in the myomas. It is suggested that PR is highly expressed in leiomyomas occurring in the reproductive period [1]. Such hormones influence rapid increase in size of leiomyoma in pregnancy which may lead to fetal wastage. However, there is lower expression of PR in EUL than in UL suggesting that different factors may contribute to the development of these tumours. Sen et al found a significant difference for labeling indices of PR between UL and EUL, however it was not significant for ER. Thus, therapeutic models targeting PRs may not be effective on EUL.
\nPatient may present with menorrhagia, or diagnosed incidentally with the history of previous myoma or myomectomy [3]. Ultrasound is useful for diagnosis of uterine fibroid. Prior diagnosis of extra-uterine fibroids is often difficult owing to non-specific clinical and radiological findings. MRI is very helpful when ultrasound shows poor delineation, and in case of rapidly growing fibroid suspicious for malignant transformation. MRI is also very useful for the diagnosis of DPL as well as to determine its extent of spread for surgical planning (Figure 1A) [3]. In case of IVL, apart from trans-vaginal ultrasound, and other modalities such as pelvic MRI, trans-thoracic echocardiography, abdomen or chest computed tomography (CT), and positron emission tomography (PET) are beneficial [2]. But there is limitation of MRI in locating retroperitoneal leiomyoma in which exact anatomical location can be often ascertained only intraoperatively [3]. Few cases may turn into leiomyosarcoma. Peritoneal cytology should be done in case of ascites [3].
\nDespite the extrauterine manifestation of leiomyoma, benign leiomyomas can be distinguished from leiomyosarcoma histologically. Sarcoma is marked by high grade cellular atypia, mitotic index of greater than 10, and presence of coagulative tumor cell necrosis [2]. IVL, usually found within uterine venous channels and microscopically shows benign appearing smooth muscle cells with low mitotic activity which stain for actin and desmin [2].
\nRecent investigations showed that IVL and BML share the same cytogenetic origin, demonstrated by comparative genomic hybridization, clonal number, and copy variance [2]. Leiomyoma and leiomyosarcoma both shows smooth muscle differentiation, however biologically they are different in relation to clinical, cytogenetic, and molecular features [13]. MED12, the mediator complex subunit 12 gene, is a recently described oncogene found in both primary and metastatic leiomyosarcoma. It is detected in as many as 70% of sporadic uterine leiomyoma [13]. Oncogenic roles of MED 12 gene is also detected in smooth muscle tumours arising in extrauterine locations, however, further validating studies required for confirming its exact role in their pathogenesis [13].
\nComplete surgical excision is considered the mainstay and definitive treatment for EULs [14]. LPD mimics carcinomatosis, so total abdominal hysterectomy along with bilateral oophorectomy is often the preferred surgical treatment [5]. However, spontaneous regression has been also described in few case reports in the literature [5]. Surgical treatment affects reproductive ability in pre-menopausal women, so it should always be planned considering the family planning of the patient. In such situation diagnosis by intra-operative frozen section is very helpful [5]. Young patient in child bearing age group, especially who shows positivity for ER or PR markers in EUL, should be subject to ovary-sparing procedures and might be benefited from adjuvant therapy using GnRH agonist [2]. In histological proven DPL cases, debulking is very effective for relieving symptoms, provided the appropriate evaluation of general health conditions of the patient [5]. In unresectable cases of EULs, a medical treatment with aromatase inhibitors, chemotherapeutic agents or a gonadotropin agonist can be considered [2, 6]. During morcellation, falling pieces of myoma fragments should be avoided and proper attention should be given during removal via the port site. Post morcellation, reverse trendelenburg position should be attempted and thorough inspection with copious peritoneal lavage is recommended to aid the removal of remnant myoma pieces [3]. The Food and Drug Administration guidelines discourage the uses of laparoscopic power morcellation during hysterectomy or myomectomy for the treatment of uterine fibroids [3].
\nA routine follow-up is advised in all the patients of uterine fibroid undergoing morcellation for the development of EUL. Similarly, a long-term follow-up is essential in all the operated cases of EUL, particularly, DPL. In EULs, recurrence, if any, usually occur within 6 months after surgical resection. Since, these tumours are hormone sensitive, they usually show regression after reduction in estrogen exposure like after attainment of menopause. Repeat surgeries for recurrent EULs usually entail greater surgical difficulty and risks including visceral injuries [3].
\nDPL may leads to peritonitis and bowel obstruction which can result into sepsis and gangrene. Also, recurrence is not unusual in DPL cases due extensive involvement of peritoneal cavity. Sometimes, malignant transformation may occur in long standing cases.
\nEULs possess a great diagnostic challenge due to abnormal locations as well as their unusual growth patterns and more commonly associated with the complications in comparison to uterine leiomyomas. Though, histologically they show similarities with their uterine counter parts, however their pathogenesis is different and yet not well understood. These EULs, are hormone sensitive and may regress automatically after the recession of hormonal sources, however, this phenomenon is not universal in all cases. Due to their higher propensity for recurrence and rare malignant transformation a close follow-up is required. A peritoneal cytology and/or frozen section examination is recommended before major surgical procedures in EULs.
\nNone to declare.
\nAuthors declare that all the necessary permissions has been obtained for using the images from the corresponding authors/editors of the concerned articles and all the papers from which these images reproduced has been cited.
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