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Research article summary (published 20 Oct 2006):

Comparing the rheology of native spider and silkworm spinning dope.

Full Abstract

Silk production has evolved to be energetically efficient and functionally optimized, yielding a material that can outperform most industrial fibres, particularly in toughness. Spider silk has hitherto defied all attempts at reproduction, despite advances in our understanding of the molecular mechanisms behind its superb mechanical properties. Spun fibres, natural and man-made, rely on the extrusion process to facilitate molecular orientation and bonding. Hence a full understanding of the flow characteristics of native spinning feedstock (dope) will be essential to translate natural spinning to artificial silk production. Here we show remarkable similarity between the rheologies for native spider-dragline and silkworm-cocoon silk, despite their independent evolution and substantial differences in protein structure. Surprisingly, both dopes behave like typical polymer melts. This observation opens the door to using polymer theory to clarify our general understanding of natural silks, despite the many specializations found in different animal species.

 

Author information

Author/s: Holland, C (C); Terry, A E (AE); Porter, D (D); Vollrath, F (F);

Affiliation: Department of Zoology, University of Oxford, South Parks Road, Oxford OX1 3PS, UK.

Journal and publication information

Publication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.

Journal: Nature materials (Nat Mater), published in England. (Language: eng)

Reference: 2006-Nov; vol 5 (issue 11) : pp 870-4

Dates: Created 2006/11/01; Completed 2006/12/12;

PMID: 17057700, status: MEDLINE (last retrieval date: 2/18/2009, IMS Date: )

Sourced from the National Library of Medicine. Abstract text and other information may be subject to copyright.

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MeSH headings (categories)

This article was linked to the MESH Headings shown below.

Associated Chemicals: Insect Proteins (0) ; Silk (0)

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