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Friday, 1 May 2009


Silk as a fiber of remarkable physical properties has attracted human attention since its origins. However it has not stopped enticing human interest and imagination over 5000 years. The more it was investigated the more mysterious its properties became. The recent developments in silk protein research has revealed its possible applications as/in  new generation of biomaterials, scaffold materials for tissue engineering, designer biomaterial for medical, commercial, and military applications, nano technology etc. The picture is still emerging. Silk will have much more in store for the ever inquisitive human mind and hopefully will tie it down more towards bio materials, in opposition to its desire to break free towards “cheaply manufacturable” synthetic materials. This however is heartening news for the silk enthusiast. Here we provide citations of 22 recent research papers on this topic. No effort has been made to arrange the papers under any particular categorization. Papers on both mulberry silk and spider silk are included.

1. Engineered disulfides improve mechanical properties of recombinant spider silk.
S Grip, J Johansson, and M Hedhammar
Protein Sci, March 16, 2009; 18(5): 1012-1022.

Nature's high-performance polymer, spider silk, is composed of specific proteins, spidroins, which form solid fibers. So far, fibers made from recombinant spidroins have failed in replicating the extraordinary mechanical properties of the native material. A recombinant miniature spidroin consisting of four poly-Ala/Gly-rich tandem repeats and a nonrepetitive C-terminal domain (4RepCT) can be isolated in physiological buffers and undergoes self assembly into macrofibers. Herein, we have made a first attempt to improve the mechanical properties of 4RepCT fibers by selective introduction of AA --> CC mutations and by letting the fibers form under physiologically relevant redox conditions. Introduction of AA --> CC mutations in the first poly-Ala block in the miniature spidroin increases the stiffness and tensile strength without changes in ability to form fibers, or in fiber morphology. These improved mechanical properties correlate with degree of disulfide formation. AA --> CC mutations in the forth poly-Ala block, however, lead to premature aggregation of the protein, possibly due to disulfide bonding with a conserved Cys in the C-terminal domain. Replacement of this Cys with a Ser, lowers thermal stability but does not interfere with dimerization, fiber morphology or tensile strength. These results show that mutagenesis of 4RepCT can reveal spidroin structure-activity relationships and generate recombinant fibers with improved mechanical properties.;19388023

2. Advancing Towards a Tissue-Engineered Tympanic Membrane: Silk Fibroin as a Substratum for Growing Human Eardrum Keratinocytes

Reza Ghassemifar, Sharon Redmond, . Zainuddin, and Traian V Chirila

Journal of Biomaterials Applications 2009, doi: 10.1177/0885328209104289

Human tympanic membrane cells (hTMCs), harvested from tympanic membrane (TM) explants, were grown in culture and then seeded on membranes prepared from silkworm (Bombyx mori) silk fibroin (BMSF) and on tissue-culture plastic membranes (PET). Fibroin was isolated from silk cast into membranes with a thickness of 10–15 µm. The hTMCs were cultured on both materials for 15 days in a serum-containing culture medium. The cells grown on both substrata were subjected to nuclear staining (DAPI) and counted. Further, the cultures were immunostained for a number of protein markers related to the epithelial/keratinocyte phenotype and cell adhesion complexes. The BMSF membranes supported levels of hTMC growth higher than that observed on the PET membranes. The immunofluorochemical analysis indicated unequivocally that BMSF is a more suitable substratum than PET with respect to the growth patterns, proliferation, and cell–cell contact and adhesion. BMSF appear as a promising substratum in the tissue-engineered constructs for the replacement of TM in case of nonhealing perforations.

3. Greatly increased toughness of infiltrated spider silk.

Lee SMPippel EGösele UDresbach CQin YChandran CVBräuniger THause GKnez M.

Science. 2009 Apr 24;324(5926):488-92

In nature, tiny amounts of inorganic impurities, such as metals, are incorporated in the protein structures of some biomaterials and lead to unusual mechanical properties of those materials. A desire to produce these biomimicking new materials has stimulated materials scientists, and diverse approaches have been attempted. In contrast, research to improve the mechanical properties of biomaterials themselves by direct metal incorporation into inner protein structures has rarely been tried because of the difficulty of developing a method that can infiltrate metals into biomaterials, resulting in a metal-incorporated protein matrix. We demonstrated that metals can be intentionally infiltrated into inner protein structures of biomaterials through multiple pulsed vapor-phase infiltration performed with equipment conventionally used for atomic layer deposition (ALD). We infiltrated zinc (Zn), titanium (Ti), or aluminum (Al), combined with water from corresponding ALD precursors, into spider dragline silks and observed greatly improved toughness of the resulting silks. The presence of the infiltrated metals such as Al or Ti was verified by energy-dispersive x-ray (EDX) and nuclear magnetic resonance spectra measured inside the treated silks. This result of enhanced toughness of spider silk could potentially serve as a model for a more general approach to enhance the strength and toughness of other biomaterials.

4. Spider silk fibers spun from soluble recombinant silk produced in mammalian cells.

Lazaris AArcidiacono SHuang YZhou JFDuguay FChretien NWelsh EASoares JWKaratzas CN.

Science. 2002 Jan 18; 295(5554):472-6

Spider silks are protein-based "biopolymer" filaments or threads secreted by specialized epithelial cells as concentrated soluble precursors of highly repetitive primary sequences. Spider dragline silk is a flexible, lightweight fiber of extraordinary strength and toughness comparable to that of synthetic high-performance fibers. We sought to "biomimic" the process of spider silk production by expressing in mammalian cells the dragline silk genes (ADF-3/MaSpII and MaSpI) of two spider species. We produced soluble recombinant (rc)-dragline silk proteins with molecular masses of 60 to 140 kilodaltons. We demonstrated the wet spinning of silk monofilaments spun from a concentrated aqueous solution of soluble rc-spider silk protein (ADF-3; 60 kilodaltons) under modest shear and coagulation conditions. The spun fibers were water insoluble with a fine diameter (10 to 40 micrometers) and exhibited toughness and modulus values comparable to those of native dragline silks but with lower tenacity. Dope solutions with rc-silk protein concentrations >20% and postspinning draw were necessary to achieve improved mechanical properties of the spun fibers. Fiber properties correlated with finer fiber diameter and increased birefringence.$=relatedarticles&logdbfrom=pubmed

5. The elaborate structure of spider silk: structure and function of a natural high performance fiber.

Römer LScheibel T.

Prion. 2008 Oct;2(4):154-61. Epub 2008 Oct 20

Universität Bayreuth, Fakultät für angew. Naturwissenschaften, Lehrstuhl für Biomaterialien, Bayreuth, Germany.

Biomaterials, having evolved over millions of years, often exceed man-made materials in their properties. Spider silk is one outstanding fibrous biomaterial which consists almost entirely of large proteins. Silk fibers have tensile strengths comparable to steel and some silks are nearly as elastic as rubber on a weight to weight basis. In combining these two properties, silks reveal a toughness that is two to three times that of synthetic fibers like Nylon or Kevlar. Spider silk is also antimicrobial, hypoallergenic and completely biodegradable. This article focuses on the structure-function relationship of the characterized highly repetitive spider silk spidroins and their conformational conversion from solution into fibers. Such knowedge is of crucial importance to understanding the intrinsic properties of spider silk and to get insight into the sophisticated assembly processes of silk proteins. This review further outlines recent progress in recombinant production of spider silk proteins and their assembly into distinct polymer materials as a basis for novel products.$=relatedreviews&logdbfrom=pubmed

6. The mechanical design of spider silks: from fibroin sequence to mechanical function.

Gosline JMGuerette PAOrtlepp CSSavage KN.

J Exp Biol. 1999 Dec;202(Pt 23):3295-303

Spiders produce a variety of silks, and the cloning of genes for silk fibroins reveals a clear link between protein sequence and structure-property relationships. The fibroins produced in the spider's major ampullate (MA) gland, which forms the dragline and web frame, contain multiple repeats of motifs that include an 8-10 residue long poly-alanine block and a 24-35 residue long glycine-rich block. When fibroins are spun into fibres, the poly-alanine blocks form (&bgr;)-sheet crystals that crosslink the fibroins into a polymer network with great stiffness, strength and toughness. As illustrated by a comparison of MA silks from Araneus diadematus and Nephila clavipes, variation in fibroin sequence and properties between spider species provides the opportunity to investigate the design of these remarkable biomaterials.

Full paper:

7. Comparative architecture of silks, fibrous proteins and their encoding genes in insects and spiders

Craig CLRiekel C.

Comp Biochem Physiol B Biochem Mol Biol. 2002 Dec;133(4):493-507

The known silk fibroins and fibrous glues are thought to be encoded by members of the same gene family. All silk fibroins sequenced to date contain regions of long-range order (crystalline regions) and/or short-range order (non-crystalline regions). All of the sequenced fibroin silks (Flag or silk from flagelliform gland in spiders; Fhc or heavy chain fibroin silks produced by Lepidoptera larvae) are made up of hierarchically organized, repetitive arrays of amino acids. Fhc fibroin genes are characterized by a similar molecular genetic architecture of two exons and one intron, but the organization and size of these units differs. The Flag, Ser (sericin gene) and BR (Balbiani ring genes; both fibrous proteins) genes are made up of multiple exons and introns. Sequences coding for crystalline and non-crystalline protein domains are integrated in the repetitive regions of Fhc and MA exons, but not in the protein glues Ser1 and BR-1. Genetic 'hot-spots' promote recombination errors in Fhc, MA, and Flag. Codon bias, structural constraint, point mutations, and shortened coding arrays may be alternative means of stabilizing precursor mRNA transcripts. Differential regulation of gene expression and selective splicing of the mRNA transcript may allow rapid adaptation of silk functional properties to different physical environments.$=relatedreviews&logdbfrom=pubmed

8. Biotechnological production of spider-silk proteins enables new applications.

Vendrely CScheibel T.

Macromol Biosci. 2007 Apr 10;7(4):401-9

The outstanding mechanical properties of spider silks have motivated many researchers to establish biotechnological production techniques which are necessary to provide sufficient amounts of silk proteins for industrial applications. Based on recent developments in genetic engineering, two strategies for the recombinant production of spider-silk proteins have been established which are discussed in detail. Further, protein-design strategies are described, enabling the combination of silk properties with additional biological, chemical, or technical features. We highlight the potential of engineered and recombinantly-produced spider-silk proteins to provide the basis for a new generation of biomaterials.

9. A protocol for the production of recombinant spider silk-like proteins for artificial fiber spinning.

Teulé FCooper ARFurin WABittencourt DRech ELBrooks ALewis RV.

Nat Protoc. 2009;4(3):341-55

The extreme strength and elasticity of spider silks originate from the modular nature of their repetitive proteins. To exploit such materials and mimic spider silks, comprehensive strategies to produce and spin recombinant fibrous proteins are necessary. This protocol describes silk gene design and cloning, protein expression in bacteria, recombinant protein purification and fiber formation. With an improved gene construction and cloning scheme, this technique is adaptable for the production of any repetitive fibrous proteins, and ensures the exact reproduction of native repeat sequences, analogs or chimeric versions. The proteins are solubilized in 1,1,1,3,3,3-hexafluoro-2-propanol (HFIP) at 25-30% (wt/vol) for extrusion into fibers. This protocol, routinely used to spin single micrometer-size fibers from several recombinant silk-like proteins from different spider species, is a powerful tool to generate protein libraries with corresponding fibers for structure-function relationship investigations in protein-based biomaterials. This protocol may be completed in 40 d.$=relatedarticles&logdbfrom=pubmed

10. Probing the elastic nature of spider silk in pursuit of the next designer fiber.

Brooks AELewis RV.

Biomed Sci Instrum. 2004;40:232-7

Spider silk, one of nature's greatest accomplishments, has a combination of strength and elasticity that is unrivaled. Spiders produce up to 7 different silks; each one with a unique combination of tensile strength and elasticity that allows the spiders' web to hold prey while being resilient enough not to break upon impact. In an attempt to determine the sequences responsible for these enviable mechanical properties, several different amino acid motifs have been defined. Much of the recent work is now concentrated on correlating amino acid motifs with a specific mechanical property. The current hypothesis is that the strength property of spider silk is conferred by a poly-alanine or alanine rich (An or GAn) motif whereas the elastic nature of spider silk is conferred by the amino acid motif, GPGXX, where X is Q, S, A, G, or Y. Despite the fact that these different motifs are now known, the combination of strength and elasticity are yet to be duplicated ex vivo. In an attempt to verify that the GPGXX motif imparts elasticity to the spider silk, the number of repeats and/or the amino acid composition of the Argiope aurantia "elastic motif" were varied and expressed in various strains of E. coli to change the elastic properties of the resulting film and/or fiber. Concurrent with work on the elasticity motif is ongoing work on the strength module. Understanding these two different motifs will aide efforts to produce a designer biomaterial for medical, commercial, and military applications.$=relatedarticles&logdbfrom=pubmed

11. Design, expression and solid-state NMR characterization of silk-like materials constructed from sequences of spider silk, Samia cynthia ricini and Bombyx mori silk fibroins.

Yang MAsakura T.

J Biochem. 2005 Jun;137(6):721-9

Silk has a long history of use in medicine as sutures. To address the requirements of a mechanically robust and biocompatible material, basic research to clarify the role of repeated sequences in silk fibroin in its structures and properties seems important as well as the development of a processing technique suitable for the preparation of fibers with excellent mechanical properties. In this study, three silk-like protein analogs were constructed from two regions selected from among the crystalline region of Bombyx mori silk fibroin, (GAGSGA)(2), the crystalline region of Samia cynthia ricini silk fibroin, (Ala)(12), the crystalline region of spider dragline silk fibroin, (Ala)(6), and the Gly-rich region of spider silk fibroin, (GGA)(4). The silk-like protein analog constructed from the crystalline regions of the spider dragline silk and B. mori silk fibroins, (A(6)SCS)(8), that constructed from the crystalline regions of the S. c.ricini and B. mori silk fibroins, (A(12)SGS)(4), that constructed from and the crystalline region of S. c.ricini silk fibroin and the glycine-rich region of spider dragline silk fibroin, (A(12)SGS)(4),were expressed their molecular weights being about 36.0 kDa, 17.0 kDa and 17.5 kDa, respectively in E. coli by means of genetic engineering technologies. (A(12)SCS)(4) and (A(12)SGS)(4 )undergo a structural transition from alpha-helix to beta-sheet on a change in the solvent treatment from trifluoroacetic acid (TFA) to formic acid (FA). However, (A(6)SCS)(8) takes on the beta-sheet structure predominantly on TFA treatment and FA treatment. Structural analysis was performed on model peptides selected from spider dragline and S. c.ricini silks by means of (13)C CP/MAS NMR.$=relatedarticles&logdbfrom=pubmed

12. Structures of Bombyx mori and Samia cynthia ricini silk fibroins studied with solid-state NMR.

Yao JNakazawa YAsakura T.

Biomacromolecules. 2004 May-Jun;5(3):680-8

There are many kinds of silks spun by silkworms and spiders, which are suitable to study the structure-property relationship for molecular design of fibers with high strength and high elasticity. In this review, we mainly focus on the structural determination of two well-known silk fibroin proteins that are from the domesticated silkworm, Bombyx mori, and the wild silkworm, Samia cynthia ricini, respectively. The structures of B. mori silk fibroin before and after spinning were determined by using an appropriate model peptide, (AG)(15), with several solid-state NMR methods; (13)C two-dimensional spin-diffusion solid-state NMR and rotational echo double resonance (REDOR) NMR techniques along with the quantitative use of the conformation-dependent (13)C CP/MAS chemical shifts. The structure of S. c. ricini silk fibroin before spinning was also determined by using a model peptide, GGAGGGYGGDGG(A)(12)GGAGDGYGAG, which is a typical repeated sequence of the silk fibroin, with the solid-state NMR methods. The transition from the structure of B. mori silk fibroin before spinning to the structure after spinning was studied with molecular dynamics calculation by taking into account several external forces applied to the silk fibroin in the silkworm.$=relatedarticles&logdbfrom=pubmed

13. Synthesis and characterization of chimeric silkworm silk.

Asakura TNitta KYang MYao JNakazawa YKaplan DL.

Biomacromolecules. 2003 May-Jun;4(3):815-20

A synthetic gene encoding a chimeric silklike protein was constructed that combined a polyalanine encoding region (Ala)(18), a sequence slightly longer than the (Ala)(12-13) found in the silk fibroin from the wild silkworm Samia cynthia ricini, and a sequence encoding GVGAGYGAGAGYGVGAGYGAGVGYGAGAGY, found in the silk fibroin from the silkworm Bombyx mori. A tetramer of the chimeric repeat sequence encoding a approximately 29 kDa protein was expressed as a fusion protein in Escherichia coli. In comparison to S. c. ricini silk, the chimeric protein demonstrated improved solubility because it could be dissolved in 8 M urea. The purified protein assumed an alpha-helical structure based on solid-state (13)C CP/MAS NMR and was less prone to conformational transition to a beta-sheet, unlike native silk proteins from S. c. ricini. Model peptides representing the crystalline region of S. c. ricini silk fibroin, (Ala)(12) and (Ala)(18), formed beta-sheet structures. Therefore, the solubility and structural transitions of the chimeric protein were significantly altered through the formation of this chimeric silk. This experimental strategy to the study of silk structure and function can be used to develop an improved understanding of the contributions of protein domains in repetitive silkworm and spider silk sequences to structure development and structural transitions.$=relatedarticles&logdbfrom=pubmed

14. Silk fibroin: structural implications of a remarkable amino acid sequence

Zhou CZConfalonieri FJacquet MPerasso RLi ZGJanin J.

Proteins. 2001 Aug 1;44(2):119-22

The amino acid sequence of the heavy chain of Bombyx mori silk fibroin was derived from the gene sequence. The 5,263-residue (391-kDa) polypeptide chain comprises 12 low-complexity "crystalline" domains made up of Gly-X repeats and covering 94% of the sequence; X is Ala in 65%, Ser in 23%, and Tyr in 9% of the repeats. The remainder includes a nonrepetitive 151-residue header sequence, 11 nearly identical copies of a 43-residue spacer sequence, and a 58-residue C-terminal sequence. The header sequence is homologous to the N-terminal sequence of other fibroins with a completely different crystalline region. In Bombyx mori, each crystalline domain is made up of subdomains of approximately 70 residues, which in most cases begin with repeats of the GAGAGS hexapeptide and terminate with the GAAS tetrapeptide. Within the subdomains, the Gly-X alternance is strict, which strongly supports the classic Pauling-Corey model, in which beta-sheets pack on each other in alternating layers of Gly/Gly and X/X contacts. When fitting the actual sequence to that model, we propose that each subdomain forms a beta-strand and each crystalline domain a two-layered beta-sandwich, and we suggest that the beta-sheets may be parallel, rather than antiparallel, as has been assumed up to now. Copyright 2001 Wiley-Liss, Inc.$=relatedreviews&logdbfrom=pubmed

15. Structural study of irregular amino acid sequences in the heavy chain of Bombyx mori silk fibroin.

Ha SWGracz HSTonelli AEHudson SM.

Biomacromolecules. 2005 Sep-Oct;6(5):2563-9

Recently, genetic studies have revealed the entire amino acid sequence of Bombyx mori silk fibroin. It is known from X-ray diffraction studies that the beta-sheet crystalline structure (silk II) of fibroin is composed of hexaamino acid sequences of GAGAGS. However, in the heavy chain of B. mori silk fibroin, there are also present 11 irregular sequences, with about 31 amino acid residues (irregular GT approximately GT sequences). The structure and role of these irregular sequences have remained unknown. One of the most frequently appearing irregular sequences was synthesized and its 3-D solution structure was studied by high-resolution 2-D NMR techniques. The 3-D structure determined for this peptide shows that it makes a loop structure (distorted omega shape), which implies that the preceding backbone direction is changed by 180 degrees, i.e., reversed, by this sequence. This may facilitate the beta-sheet formation between the crystal-forming building blocks, GAGAGS/GY approximately GY sequences, in the fibroin heavy chain.$=relatedarticles&logdbfrom=pubmed

16. New silk protein: modification of silk protein by gene engineering for production of biomaterials

Mori HTsukada M.

J Biotechnol. 2000 Aug;74(2):95-103

The interest in silk fibroin morphology and structure have increased due to its attractiveness for bio-related applications. Silk fibers have been used as sutures for a long time in the surgical field, due to the biocompatibility of silk fibroin fibers with human living tissue. In addition, it has been demonstrated that silk can be used as a substrate for enzyme immobilization in biosensors. A more complete understanding of silk structure would provide the possibility to further exploit silk fibroin for a wide range of new uses, such as the production of oxygen-permeable membranes and biocompatible materials. Silk fibroin-based membranes could be utilized as soft tissue compatible polymers. Baculovirus-mediated transgenesis of the silkworm allows specific alterations in a target sequence. Homologous recombination of a foreign gene downstream from a powerful promoter, such as the fibroin promoter, would allow the constitutive production of a useful protein in the silkworm and the modification of the character of silk protein. A chimeric protein consisted of fibroin and green fluorescent protein was expressed under the control of fibroin in the posterior silk gland and the gene product was spun into the cocoon layer. This technique, gene targeting, will lead to the modification and enhancement of physicochemical properties of silk protein.$=relatedreviews&logdbfrom=pubmed

17. Silk fibroin protein from mulberry and non-mulberry silkworms: cytotoxicity, biocompatibility and kinetics of L929 murine fibroblast adhesion

Acharya CGhosh SKKundu SC.

J Mater Sci Mater Med. 2008 Aug;19(8):2827-36. Epub 2008 Mar 6

Silks fibers and films fabricated from fibroin protein of domesticated mulberry silkworm cocoon have been traditionally utilized as sutures in surgery and recently as biomaterial films respectively. Here, we explore the possibility of application of silk fibroin protein from non-mulberry silkworm cocoon as a potential biomaterial aid. In terms of direct inflammatory potential, fibroin proteins from Antheraea mylitta and Bombyx mori are immunologically inert and invoke minimal immune response. Stimulation of murine peritoneal macrophages and RAW 264.7 murine macrophages by these fibroin proteins both in solution and in the form of films assayed in terms of nitric oxide and TNFalpha production showed comparable stimulation as in collagen. Kinetics of adhesion of L929 murine fibroblasts, for biocompatibility evaluation, monitored every 4 h from seeding and studied over a period of 24 h, reveal A. mylitta fibroin film to be a better substrate in terms of rapid and easier cellularization. Cell viability studies by MTT assay and flow cytometric analyses indicate the ability of fibroin matrices to support cell growth and proliferation comparable to collagen for long-term culture. This matrix may have potential to serve in those injuries where rapid cellularization is essential.$=relatedarticles&logdbfrom=pubmed

18. Growth of human cells on a non-woven silk fibroin net: a potential for use in tissue engineering.

Unger REWolf MPeters KMotta AMigliaresi CJames Kirkpatrick C.

Biomaterials. 2004 Mar;25(6):1069-75

We have examined a novel biomaterial consisting of a non-woven fibroin net produced from silk (Bombyx mori) cocoons for its ability to support the growth of human cells. Various human cells of different tissue and cell types (endothelial, epithelial, fibroblast, glial, keratinocyte, osteoblast) were examined for adherence and growth on the nets by confocal laser microscopy after staining of the cells with calcein-AM and by electron microscopy. All the cells readily adhered and spread over the individual fibers of the nets. Most of the cells were able to grow and survive on the nets for at least 7 weeks and growth not only covered the individual fibers of the net but generally bridged the gaps between individual fibers forming tissue-like structures. Scanning electron microscopic examination of the nets demonstrated a tight association of individual cells with the fibers and nets examined after removal of cells showed no evidence that the growth of cells in any way changed the structure of the fibers. Thus, silk fibroin nets are highly human cell-compatible and should be a useful new scaffolding biomaterial applicable for a wide range of target tissues in addition to supporting endothelial cells required for the vascularization of the newly formed tissue.$=relatedarticles&logdbfrom=pubmed

19. Molecular mechanisms of spider silk.

Hu XVasanthavada KKohler KMcNary SMoore AMVierra CA.

Cell Mol Life Sci. 2006 Sep;63(17):1986-99

Spiders spin high-performance silks through the expression and assembly of tissue-restricted fibroin proteins. Spider silks are composite protein biopolymers that have complex microstructures. Retrieval of cDNAs and genomic DNAs encoding silk fibroins has revealed an association between the protein sequences and structure-property relationships. However, before spider silks can be subject to genetic engineering for commercial applications, the complete protein sequences and their functions, as well as the details of the spinning mechanism, will require additional progress and collaborative efforts in the areas of biochemistry, molecular biology and material science. Novel approaches to reveal additional molecular constituents embedded in the spider fibers, as well as cloning strategies to manipulate the genes for expression, will continue to be important aspects of spider biology research. Here we summarize the molecular characteristics of the different spider fibroins, the mechanical properties and assembly process of spidroins and the advances in protein expression systems used for recombinant silk production. We also highlight different technical approaches being used to elucidate the molecular constituents of silk fibers.

20. Silk-based biomaterials.

Altman GHDiaz FJakuba CCalabro THoran RLChen JLu HRichmond JKaplan DL.

Biomaterials. 2003 Feb;24(3):401-16

Silk from the silkworm, Bombyx mori, has been used as biomedical suture material for centuries. The unique mechanical properties of these fibers provided important clinical repair options for many applications. During the past 20 years, some biocompatibility problems have been reported for silkworm silk; however, contamination from residual sericin (glue-like proteins) was the likely cause. More recent studies with well-defined silkworm silk fibers and films suggest that the core silk fibroin fibers exhibit comparable biocompatibility in vitro and in vivo with other commonly used biomaterials such as polylactic acid and collagen. Furthermore, the unique mechanical properties of the silk fibers, the diversity of side chain chemistries for 'decoration' with growth and adhesion factors, and the ability to genetically tailor the protein provide additional rationale for the exploration of this family of fibrous proteins for biomaterial applications. For example, in designing scaffolds for tissue engineering these properties are particularly relevant and recent results with bone and ligament formation in vitro support the potential role for this biomaterial in future applications. To date, studies with silks to address biomaterial and matrix scaffold needs have focused on silkworm silk. With the diversity of silk-like fibrous proteins from spiders and insects, a range of native or bioengineered variants can be expected for application to a diverse set of clinical needs.

21. Skeletal tissue engineering using silk biomaterials

MacIntosh ACKearns VRCrawford AHatton PV.

J Tissue Eng Regen Med. 2008 Mar-Apr;2(2-3):71-80

Silks have been proposed as potential scaffold materials for tissue engineering, mainly because of their physical properties. They are stable at physiological temperatures, flexible and resist tensile and compressive forces. Bombyx mori (silkworm) cocoon silk has been used as a suture material for over a century, and has proved to be biocompatible once the immunogenic sericin coating is removed. Spider silks have a similar structure to silkworm silk but do not have a sericin coating. This paper provides a general overview on the use of silk protein in biomaterials, with a focus on skeletal tissue engineering.

22. Spider silks and their applications

Kluge JARabotyagova OLeisk GGKaplan DL.

Trends Biotechnol. 2008 May;26(5):244-51. Epub 2008 Mar 25

Spider silks are characterized by remarkable diversity in their chemistry, structure and functions, ranging from orb web construction to adhesives and cocoons. These unique materials have prompted efforts to explore potential applications of spider silk equivalent to those of silkworm silks, which have undergone 5,000 years of domestication and have a variety of uses, from textiles to biomedical materials. Recent progress in genetic engineering of spider silks and the development of new chimeric spider silks with enhanced functions and specific characteristics have advanced spider silk technologies. Further progress in yields of expressed spider-silk proteins, in the control of self-assembly processes and in the selective exploration of material applications is anticipated in the future. The unique features of spider silks, the progress and challenges in the cloning and expression of these silks, environmentally triggered silk assembly and disassembly and the formation of fibers, films and novel chimeric composite materials from genetically engineered spider silks will be reviewed.


1 comment:

Dr. Panomir Tzenov, President, BACSA said...

Dear Dr Rajesh,
On behalf of all BACSA members and myself too I would like congratulate you with your very useful blog – The silkworm and also to express our due gratitude about your activity for the benefits of the world sericulture community!
I am sending you attached a review on the use of sericulture products for non – textile purposes which may be of interest.
With best regards!
Dr P. Tzenov
President of BACSA

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