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Proceedings of the Royal Society B: Biological Sciences logoLink to Proceedings of the Royal Society B: Biological Sciences
. 2004 Feb 7;271(1536):291–299. doi: 10.1098/rspb.2003.2591

Molecular design of the alpha-keratin composite: insights from a matrix-free model, hagfish slime threads.

Douglas S Fudge 1, John M Gosline 1
PMCID: PMC1691592  PMID: 15058441

Abstract

We performed mechanical tests on a matrix-free keratin model-hagfish slime threads-to test the hypothesis that intermediate filaments (IFs) in hydrated hard alpha-keratins are maintained in a partly dehydrated state. This hypothesis predicts that dry IFs should possess mechanical properties similar to the properties of hydrated hard alpha-keratins, and should swell more than hard alpha-keratins in water. Mechanical and swelling measurements of hagfish threads were consistent with both of these predictions, suggesting that an elastomeric keratin matrix resists IF swelling and keeps IF stiffness and yield stress high. The elastomeric nature of the matrix is indirectly supported by the inability of matrix-free IFs (i.e. slime threads) to recover from post-yield deformation. We propose a general conceptual model of the structural mechanics of IF-based materials that predicts the effects of hydration and cross-linking on stiffness, yield stress and extensibility.

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Selected References

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