Evidence from flagelliform silk cDNA for the structural basis of elasticity and modular nature of spider silks 1 1Edited by M. F. Moody

Hayashi, Cheryl Y.; Lewis, Randolph V.

doi:10.1006/jmbi.1997.1478

Cited by 344 publications

(325 citation statements)

References 39 publications

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“…This strategy has provided new opportunities in fundamental studies of spider silk genetics, silk protein structure and function, and materials processing [2,[4][5][6]. In general, interest in spider silk has increased in recent years due to the differences in mechanical properties when compared to silkworm silk and the presence of the multi-gene family encoding this group of silks as a basis for the study of protein structurefunction relationships [4,[6][7][8][9][10][11].…”

Section: Spider Silksmentioning

confidence: 99%

“…Cloning and expression of native and synthetic silks has been achieved in a variety of host systems. The sequences of cDNAs and genomic clones encoding spider silks illustrate the highly repetitive structures [4,6,[8][9][10][11], which can be readily exploited to construct genetically engineered spider silk-like proteins using synthetic oligonucleotide versions of the consensus repeats or variants of these repeats. This highly repetitive sequence was also recently fully described for the fibroin heavy chain from the silkworm, B. mori [12].…”

Section: Spider Silksmentioning

confidence: 99%

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Silk-based biomaterials

et al. 2003

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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. r

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Section: Spider Silksmentioning

confidence: 99%

Section: Spider Silksmentioning

confidence: 99%

Silk-based biomaterials

et al. 2003

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“…To assign correspondence between our N. clavipes spidroins and those previously described, we performed alignments of conserved N-and C-terminal sequences and internal motifs reported to be specific to a particular spidroin class [43][44][45] . Most of our N. clavipes Fig.…”

Section: An Annotated Genome For N Clavipesmentioning

confidence: 99%

“…1). N. clavipes spidroins were outliers in their amino acid frequencies relative to all other predicted genes in the N. clavipes genome, being notably enriched for glycine (20.1%, Wilcoxon rank-sum test, P = 2.8 × 10 −15 ), alanine (14.6%, P = 2.6 × 10 −8 ), and serine (11.6%, P = 8.5 × 10 −4 ) residues found in known repeated motifs: (GA) n , (A) n (polyalanine), and GGX (where X = A, S, or Y) 44 ( Supplementary Figs. 5 and 6).…”

Section: An Annotated Genome For N Clavipesmentioning

confidence: 99%

The Nephila clavipes genome highlights the diversity of spider silk genes and their complex expression

et al. 2017

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More than 380 million years of evolution have produced >46,000 extant spider species, exhibiting an incredible diversity of silks used for prey capture and reproduction [1][2][3] . Spider silks can be stronger than steel and tougher than Kevlar, yet are much lighter weight than these manmade materials 4 . Silks vary in extensibility 5 , are temperature resilient 6 , can enable electrical conduction 7 , and can inhibit bacterial growth while being nearly invisible to the human immune system 8 . Thus, novel materials derived from spider silks offer tremendous potential for medical and industrial innovation. To take advantage of their desirable properties, we must learn more about spider silk genetic structure, functional diversity, and production.A female orb-weaving spider can have up to seven morphologically differentiated types of silk glands, each believed to extrude a distinct class of silk with biophysical characteristics resulting from the expression of a unique combination of silk genes in that gland 9,10 . The silk classes of a typical 'gluey silk' orb-weaver (Araneoidea) female include (i) major ampullate silk, which exhibits great tensile strength and is employed in draglines, bridgelines, and web radii 11,12 ; (ii) minor ampullate silk, used for inelastic temporary spirals during web building 11,12 ; (iii) cement-like piriform silk that bonds fibers together and to other substrates 13,14 ; (iv) strong, yet flexible aciniform silk used for prey wrapping and egg case insulation 15 ; (v) tubuliform and cylindriform silk that constitutes the tough outer layer of egg cases 16,17 ; (vi) flagelliform silk that exhibits unparalleled extensibility and is used in the capture spiral 18,19 ; and (vii) the viscous and sticky aggregate silk that aids in prey capture [20][21][22][23][24] . Many spider species produce just a subset of these silk classes, and some produce yet other silk types, including cribellate silk 25 . Each species possesses an assortment of specialized gland types that are thought to produce distinct classes of silks to fit specific needs 9,26,27 .Spider silks are composed primarily of spidroin proteins (where a 'spidroin' is a spider fibroin [28][29][30][31] ) that, by convention, have been named and classified according to the specific silk gland in which they were first discovered. Spidroin proteins have conserved N-and C-terminal domains that flank long runs of repeated motifs 32-34 , the composition and number of which confer specific physical properties to silks 27 . Yet, despite decades of research on orb-weaver silks, there is incomplete knowledge of all the spidroins within an orb-weaver species.Adding to the sampling of sequences obtained from targeted investigations, the assembly of the velvet spider (Stegodyphus mimosarum) genome yielded 19 spidroins, the largest collection from any single species 27 . Owing to the challenges of assembling arrays of repeats, several of the S. mimosarum spidroin sequences are incomplete, without the sequences encoding N-and C-terminal domains anchored ...

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“…27 The repeating GPGGX blocks, which were previously identified in dragline silk but not found in other less elastic silks, have been identified in flagelliform silk. 28 Protein and amino acid composition of silks from the black widow spider (Latrodectus hesperus) show variation between dragline, inner egg case, and scaffolding silks. 29 The inner silk of the egg case contains a higher proportion of Ala compared with Gly, possibly being high in crystalline -sheet content for strength to protect the eggs.…”

Section: Introductionmentioning

confidence: 99%

Orientational order of Australian spider silks as determined by solid‐state NMR

et al. 2006

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A simple solid-state NMR method was used to study the structure of 13 C-and 15 Nenriched silk from two Australian orb-web spider species, Nephila edulis and Argiope keyserlingi. Carbon-13 and 15 N spectra from alanine-or glycine-labeled oriented dragline silks were acquired with the fiber axis aligned parallel or perpendicular to the magnetic field. The fraction of oriented component was determined from each amino acid, alanine and glycine, using each nucleus independently, and attributed to the ordered crystalline domains in the silk. The relative fraction of ordered alanine was found to be higher than the fraction of ordered glycine, akin to the observation of alanine-rich domains in silk-worm (Bombyx mori) silk. A higher degree of crystallinity was observed in the dragline silk of N. edulis compared with A. keyserlingi, which correlates with the superior mechanical properties of the former #

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Evidence from flagelliform silk cDNA for the structural basis of elasticity and modular nature of spider silks 1 1Edited by M. F. Moody

Cited by 344 publications

References 39 publications

Silk-based biomaterials

Silk-based biomaterials

The Nephila clavipes genome highlights the diversity of spider silk genes and their complex expression

Orientational order of Australian spider silks as determined by solid‐state NMR

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