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Molecular Order in Silk Secretions

Published online by Cambridge University Press:  25 February 2011

Christopher Viney,
Keven Kerkam,
Lisa Gilliland,
David Kaplan and
Stephen Fossey
Christopher Viney
Affiliation:
Molecular Bioengineering Program, Center for Bioengineering WD-12, Univ. of Washington, Seattle, WA 98195
Keven Kerkam
Affiliation:
Dept. of Materials Science and Engineering FB-10, Univ. of Washington, Seattle, WA 98195
Lisa Gilliland
Affiliation:
Oncogen/Bristol Myers Squibb, 3005 First Avenue, Seattle, WA 98121
David Kaplan
Affiliation:
US Army Research, Development and Engineering Center, Natick, MA 01760
Stephen Fossey
Affiliation:
US Army Research, Development and Engineering Center, Natick, MA 01760
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Abstract

Transmitted polarized light microscopy of various natural silk secretions reveals their ability to form nematic liquid crystalline phases. Observations of microstructure, together with a simple secondary structure analysis of known amino acid sequences in silk proteins, suggest that the rodlike structures forming the nematic phase are supramolecular aggregates, rather than individual rigid molecular segments. The optical birefringence of dragline fiber produced by controlled silking depends on the linear haul-off velocity, and can exceed the birefringence of naturally spun fibers; this suggests the possibility of in-vitro spinning of silk to obtain values of strength and stiffness even greater than those achieved in vivo.

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Type
Research Article
Information
MRS Online Proceedings Library (OPL) , Volume 248: Symposium O – Complex Fluids , 1991, 89
Copyright
Copyright © Materials Research Society 1992

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