A structural view on spider silk proteins and their role in fiber assembly

Journal of Peptide Science : an Official Publication of the European Peptide Society
Franz Hagn

Abstract

Spider silk is the toughest known biomaterial and even outrivals modern synthetic high-performance materials. The question of understanding fiber formation is how the spider can prevent premature and fatal aggregation processes inside its own body and how the chemical and mechanical stimuli used to induce the fiber formation process translate into structural changes of the silk material, finally leading to controlled and irreversible aggregation. Here, the focus will be on the structure and function of the highly conserved N-domains and C-terminal domains of spider dragline silk which, unlike the very long repetitive sequence elements, adopt a folded conformation in solution and are therefore able to control intermolecular interactions and aggregation between other spider silk molecules. The structures of these domains add valuable details for the construction of a molecular picture of the complicated and highly optimized silk assembly process that might be beneficial for large-scale in vitro fiber formation attempts with recombinant silk material.

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Citations

Oct 16, 2015·Advanced Healthcare Materials·Yihua LooAnna Mitraki
Oct 27, 2015·Frontiers in Microbiology·Guanghong ZengDaniel E Otzen
Jul 12, 2016·ACS Biomaterials Science & Engineering·Davoud EbrahimiMarkus J Buehler
Jun 18, 2016·Scientific Reports·Katarzyna JastrzebskaHanna Dams-Kozlowska
Jan 16, 2014·Biomacromolecules·Shujing WangDaiwen Yang

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