Spider Silk:  Ancient Ideas for New Biomaterials

Lewis, Randolph V.

doi:10.1021/cr010194g

Cited by 350 publications

(376 citation statements)

References 53 publications

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“…Each polypeptide repeat therefore has distinct functional features resulting in the outstanding mechanical properties of spider silk threads. 15 based on the areas with low electron density, which are characterized by amorphous structures with few defined elements of secondary or supersecondary structure. 40, 41 Such arrangement closely resembles that of protein hydrogels.…”

Section: The Structure Of Spider Silkmentioning

confidence: 99%

“…In nature, spiders draw the thread with the hind legs (or by the force of gravity in case of roping) out of the spinning wart. 15,36,37 This drawing process has been copied in the laboratory by forced silking of captive spiders. Analysis of the silking process revealed that spinning speeds range from 0.1 to 400 mm per second.…”

Section: Gpggx/gpgqq [Iii] Ggx (X = a S Or Y) And [Iv]mentioning

confidence: 99%

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The elaborate structure of spider silk

Römer

Scheibel

2008

Prion

292

179

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Section: The Structure Of Spider Silkmentioning

confidence: 99%

Section: Gpggx/gpgqq [Iii] Ggx (X = a S Or Y) And [Iv]mentioning

confidence: 99%

The elaborate structure of spider silk

Römer

Scheibel

2008

Prion

292

179

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“…The silk proteins' sophisticated structure and carefully guided folding, self-organization and phase segregation during the spinning process allows these different structural motifs to coexist in the final material. In this way, the versatile properties of different types of silk materials are precisely tailored according to their function [11][12][13] . Inspired by this example of nature's design principles, the selective formation of onedimensional nanostructures from b-sheet-forming oligopeptides and oligopeptide-modified polymers has been extensively investigated [14][15][16][17][18][19][20][21][22][23][24][25][26][27][28] .…”

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confidence: 99%

A toolbox of oligopeptide-modified polymers for tailored elastomers

Croisier

Schweizer

et al. 2014

Nat Commun

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Biomaterials are constructed from limited sets of building blocks but exhibit extraordinary and versatile properties, because hierarchical structure formation lets them employ identical supramolecular motifs for different purposes. Here we exert a similar degree of structural control in synthetic supramolecular elastomers and thus tailor them for a broad range of thermomechanical properties. We show that oligopeptide-terminated polymers selectively self-assemble into small aggregates or nanofibrils, depending on the length of the oligopeptides. This process is self-sorting if differently long oligopeptides are combined so that different nanostructures coexist in bulk mixtures. Blends of polymers with oligopeptides matching in length furnish reinforced elastomers that exhibit shear moduli one order of magnitude higher than the parent polymers. By contrast, novel interpenetrating supramolecular networks that display excellent vibration damping properties are obtained from blends comprising non-matching oligopeptides or unmodified polymers. Hence, blends of oligopeptide-modified polymers constitute a toolbox for tailored elastomers with versatile properties.

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“…Perhaps even more impressive is the spinning process in which the spider silk proteins (spidroins) are assembled from a highly soluble storage state into a well ordered and insoluble fiber. Spiders can produce up to seven different types of silk each composed of different spidroin proteins and spun from distinct abdominal glands (1). Here, the spinning process of the major ampullate gland of Nephila spiders will be summarized as an example, but many of its features are common to other spider silks and are even analogous to moth and butterfly silks.…”

mentioning

confidence: 99%

Spidroin N-terminal Domain Promotes a pH-dependent Association of Silk Proteins during Self-assembly

Gaines

Sehorn

Marcotte

2010

Journal of Biological Chemistry

126

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Spider silks are spun from concentrated solutions of spidroin proteins. The appropriate timing of spidroin assembly into organized fibers must be highly regulated to avoid premature fiber formation. Chemical and physical signals presented to the silk proteins as they pass from the ampulle and through the tapered duct include changes in ionic environment and pH as well as the introduction of shear forces. Here, we show that the N-terminal domain of spidroins from the major ampullate gland (MaSp-NTDs) for both Nephila and Latrodectus spiders associate noncovalently as homodimers. The MaSp-NTDs are highly pH-responsive and undergo a structural transition in the physiological pH range of the spider duct. Tryptophan fluorescence of the MaSp-NTDs reveals a change in conformation when pH is decreased, and the pH at which the transition occurs is determined by the amount and type of salt present. Size exclusion chromatography and pulldown assays both indicate that the lower pH conformation is associated with a significantly increased MaSp-NTD homodimer stability. By transducing the duct pH signal into specific protein-protein interactions, this conserved spidroin domain likely contributes significantly to the silk-spinning process. Based on these results, we propose a model of spider silk assembly dynamics as mediated through the MaSp-NTD.

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Spider Silk: Ancient Ideas for New Biomaterials

Cited by 350 publications

References 53 publications

The elaborate structure of spider silk

The elaborate structure of spider silk

A toolbox of oligopeptide-modified polymers for tailored elastomers

Spidroin N-terminal Domain Promotes a pH-dependent Association of Silk Proteins during Self-assembly

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