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Issue 5, 2006
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Spider silk as archetypal protein elastomer

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We present an overview of the physical properties of spider silks, and introduce a model designed to study the energy absorbed by the material as it stretches before breaking. Of particular interest are the inter- and intramolecular hydrogen bonds as well as the role of water in modifying the material properties of silk. A solid understanding of this interaction is of paramount importance for any deeper insights into the mechanical properties of any biomaterial. Here we note that the typical biological material has evolved to function in the fully hydrated i.e. elastomeric state. We conclude that silk after its transformation from the hydrated feedstock to the dehydrated fibre state can in fact be analysed in great detail and interpreted as representative of a wide range of elastomeric proteins covering, inter alia, bone, keratins, elastin and collagen.

Graphical abstract: Spider silk as archetypal protein elastomer

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The article was received on 04 Jan 2006, accepted on 06 Mar 2006 and first published on 29 Mar 2006

Article type: Review Article
DOI: 10.1039/B600098N
Soft Matter, 2006,2, 377-385

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    Spider silk as archetypal protein elastomer

    F. Vollrath and D. Porter, Soft Matter, 2006, 2, 377
    DOI: 10.1039/B600098N

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