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Journal of Experimental Biology, Vol 202, Issue 23 3295-3303, Copyright © 1999 by Company of Biologists
JOURNAL ARTICLES |
JM Gosline, PA Guerette, CS Ortlepp and KN Savage
Department of Zoology, University of British Columbia, Vancouver, British Columbia, Canada V6T 1Z4. gosline@zoology.ubc.ca
Spiders produce a variety of silks, and the cloning of genes for silk fibroins reveals a clear link between protein sequence and structure-property relationships. The fibroins produced in the spider's major ampullate (MA) gland, which forms the dragline and web frame, contain multiple repeats of motifs that include an 8-10 residue long poly-alanine block and a 24-35 residue long glycine-rich block. When fibroins are spun into fibres, the poly-alanine blocks form (&bgr;)-sheet crystals that crosslink the fibroins into a polymer network with great stiffness, strength and toughness. As illustrated by a comparison of MA silks from Araneus diadematus and Nephila clavipes, variation in fibroin sequence and properties between spider species provides the opportunity to investigate the design of these remarkable biomaterials.
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