This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com
Invited Review
The coiled coil silk of bees, ants, and hornets †
Article first published online: 9 AUG 2011
DOI: 10.1002/bip.21702
Copyright © 2011 Wiley Periodicals, Inc.
Issue

Biopolymers
Special Issue: Silks: Properties and Uses of Natural and Designed Variants
Volume 97, Issue 6, pages 446–454, June 2012
Additional Information
How to Cite
Sutherland, T. D., Weisman, S., Walker, A. A. and Mudie, S. T. (2012), The coiled coil silk of bees, ants, and hornets . Biopolymers, 97: 446–454. doi: 10.1002/bip.21702
- †
Publication History
- Issue published online: 20 MAR 2012
- Article first published online: 9 AUG 2011
- Manuscript Accepted: 27 JUL 2011
- Manuscript Revised: 26 JUL 2011
- Manuscript Received: 29 JUN 2011
Funded by
- Australian Synchrotron Research Program
- Abstract
- Article
- References
- Cited By
Keywords:
- coiled coil;
- recombinant proteins;
- hymenoptera;
- labial gland;
- silk
Abstract
In this article, we review current knowledge about the silk produced by the larvae of bees, ants, and hornets [Apoidea and Vespoidea: Hymenoptera]. Different species use the silk either alone or in composites for a variety of purposes including mechanical reinforcement, thermal regulation, or humidification. The characteristic molecular structure of this silk is α-helical proteins assembled into tetrameric coiled coils. Gene sequences from seven species are available, and each species possesses a copy of each of four related silk genes that encode proteins predicted to form coiled coils. The proteins are ordered at multiple length scales within the labial gland of the final larval instar before spinning. The insects control the morphology of the silk during spinning to produce either fibers or sheets. The silk proteins are small and non repetitive and have been produced artificially at high levels by fermentation in E. coli. The artificial silk proteins can be fabricated into materials with structural and mechanical properties similar to those of native silks. © 2011 Wiley Periodicals, Inc. Biopolymers 97: 446–454, 2012.

1097-0282/asset/BIP_left.gif?v=1&s=f807857598ff440ee8acab64bad01b412bcbb591)