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First published online May 30, 2008
Journal of Experimental Biology 211, 1948-1957 (2008)
Published by The Company of Biologists 2008
doi: 10.1242/jeb.014225

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The role of proline in the elastic mechanism of hydrated spider silks

Ken N. Savage and John M. Gosline^*

Department of Zoology, 6270 University Boulevard, University of British Columbia, Vancouver, British Columbia, Canada, V6K 1Z4

^* Author for corresponding (e-mail: gosline{at}zoology.ubc.ca)

Accepted 5 April 2008

This study used thermoelastic measurements to investigate the role of proline in the elastic mechanism of hydrated, spider major ampullate (MA) and flagelliform (FL) silks. Experiments on hydrated MA silk from Araneus diadematus (proline content 16%) reveal that conformational entropy elasticity accounts for about 90% of the elastic force at small extensions, but entropy elasticity drops to about half by 50% extension. The decrease in the entropic component with extension is due to the presence of relatively short and conformationally restricted network chains in Araneus MA silk. Experiments on hydrated Araneus FL silk (proline content 16%) indicate that entropy elasticity dominates the elastic mechanism up to extensions of 100% and beyond, which likely reflects the fact that the glycine-rich network chains in FL silk are longer and less conformationally restricted than those in the MA silk. Thus, the rubber-like, entropic elasticity of these two proline-rich silks is consistent with networks of amorphous chains that become mobile when hydrated. By contrast, the elastic mechanism of hydrated Nephila clavipes MA silk (proline content 3.5%) shows a small contribution from entropic elasticity for extensions of 5% or less, and by 10% extension the elastic force is due entirely to bond-energy elasticity, probably associated with the deformation of stable secondary structures. These results indicate that there are major differences in the structural organization of the glycine-rich network chains and the mechanism of elasticity in proline-rich and proline-deficient fibroins.

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