Silverfish silk is formed by entanglement of randomly coiled protein chains

Walker, Andrew A., Church, Jeffrey S., Woodhead, Andrea L. and Sutherland, Tara D. (2013) Silverfish silk is formed by entanglement of randomly coiled protein chains. Insect Biochemistry and Molecular Biology, 43 7: 572-579. doi:10.1016/j.ibmb.2013.03.014

Author Walker, Andrew A.
Church, Jeffrey S.
Woodhead, Andrea L.
Sutherland, Tara D.
Title Silverfish silk is formed by entanglement of randomly coiled protein chains
Journal name Insect Biochemistry and Molecular Biology   Check publisher's open access policy
ISSN 0965-1748
Publication date 2013
Year available 2013
Sub-type Article (original research)
DOI 10.1016/j.ibmb.2013.03.014
Open Access Status
Volume 43
Issue 7
Start page 572
End page 579
Total pages 8
Place of publication Kidlington, Oxford, United Kingdom
Publisher Pergamon Press
Collection year 2014
Language eng
Subject 1303 Specialist Studies in Education
1312 Molecular Biology
1109 Neurosciences
Abstract Silks are semi-crystalline solids in which protein chains are associated by intermolecular hydrogen bonding within ordered crystallites, and by entanglement within unordered regions. By varying the type of protein secondary structure within crystallites and the overall degree of molecular order within fibers, arthropods produce fibers with a variety of physical properties suited to many purposes. We characterized silk produced as a tactile stimulus during mating by the grey silverfish (Ctenolepisma longicaudata) using Fourier transform infrared spectroscopy, polarized Raman spectroscopy, gel electrophoresis and amino acid analysis. Fibers were proteinaceous-the main component being a 220kDa protein-and were rich in Gln/Glu, Leu, and Lys. The protein structure present was predominantly random coil, with a lesser amount of beta-structure. Silk fibers could readily be solubilized in aqueous solutions of a mild chaotrope, sodium dodecyl sulfate, indicating protein chains were not cross-linked by disulfide or other covalent bonds. We conclude that entanglement is the major mechanism by which these silk proteins cohere into a solid material. We propose silks used as short-term tactile cues are subject to less stringent requirements for molecular order relative to other silks, allowing the random coil structure to be favored as an adaptation promoting maximal entanglement and adhesion.
Keyword Apterygote
Raman spectroscopy
Random coil
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Non HERDC
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