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Distinct contributions of model MaSp1 and MaSp2 like peptides to the mechanical properties of synthetic major ampullate silk fibers as revealed in silico
Authors Brooks AE, Nelson SR, Jones JA, Koenig C, Hinman M, Stricker S, Lewis RV
Published 21 August 2008 Volume 2008:1 Pages 9—16
DOI https://doi.org/10.2147/NSA.S3961
Review by Single anonymous peer review
Peer reviewer comments 3
Amanda E Brooks, Shane R Nelson, Justin A Jones, Courtney Koenig, Michael Hinman, Shane Stricker, Randolph V Lewis
Department of Molecular Biology, University of Wyoming, Laramie, WY, USA
Abstract: All characterized major ampullate silks from orb-web weaving spiders are composites of primarily two different proteins: MaSp1 and MaSp2. The conserved association of MaSp1 and MaSp2 in these spider species, the highly conserved amino acid motifs, and variable ratios of MaSp1 to MaSp2 demonstrate the importance of both MaSp1 and MaSp2 to the strength and elasticity of the fiber. Computer simulated mechanical tests predicted differing roles for MaSp1 and MaSp2 in the mechanical properties of the fibers. Recombinant MaSp1 and MaSp2 proteins were blended and spun into fibers mimicking the computer-simulated conditions. Mechanical testing verified the differing roles of MaSp1 and MaSp2.
Keywords: spider silk, mechanical properties, MaSp1, MaSp2
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