Article abstract
Nature Materials 2, 278 - 283 (2003)
Published online: 23 March 2003 | doi:10.1038/nmat858
Subject Categories: Biological materials | Semiconductors
Molecular nanosprings in spider capture-silk threads
Nathan Becker1, Emin Oroudjev1, Stephanie Mutz1, Jason P. Cleveland2, Paul K. Hansma1, Cheryl Y. Hayashi3, Dmitrii E. Makarov4 & Helen G. Hansma1
Abstract
Spider capture silk is a natural material that outperforms almost any synthetic material in its combination of strength and elasticity. The structure of this remarkable material is still largely unknown, because spider-silk proteins have not been crystallized. Capture silk is the sticky spiral in the webs of orb-weaving spiders. Here we are investigating specifically the capture spiral threads from Araneus, an ecribellate orb-weaving spider. The major protein of these threads is flagelliform protein, a variety of silk fibroin. We present models for molecular and supramolecular structures of flagelliform protein, derived from amino acid sequences, force spectroscopy (molecular pulling) and stretching of bulk capture web. Pulling on molecules in capture-silk fibres from Araneus has revealed rupture peaks due to sacrificial bonds, characteristic of other self-healing biomaterials. The overall force changes are exponential for both capture-silk molecules and intact strands of capture silk.
- Department of Physics, University of California, Santa Barbara, California 93106, USA
- Asylum Research, 341 Bolay Drive, Santa Barbara, California 93117, USA
- Department of Biology, University of California, Riverside, California 92521, USA
- Department of Chemistry and Biochemistry and Institute for Theoretical Chemistry, University of Texas at Austin, Austin, Texas 78712, USA
Correspondence to: Helen G. Hansma1 e-mail: hhansma@physics.ucsb.edu
|
MORE ARTICLES LIKE THIS These links to content published by NPG are automatically generated NEWS AND VIEWS RESEARCH |
