4.2 Review

The role of terminal domains during storage and assembly of spider silk proteins

Journal

BIOPOLYMERS
Volume 97, Issue 6, Pages 355-361

Publisher

WILEY
DOI: 10.1002/bip.22006

Keywords

spider silk; biomaterials; silk assembly; non-repetitive termini; fibrous proteins

Funding

  1. US Army [W911NF-08-1-0284]
  2. DFG [SCHE603/4-4]

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Fibrous proteins in nature fulfill a wide variety of functions in different structures ranging from cellular scaffolds to very resilient structures like tendons and even extra-corporal fibers such as silks in spider webs or silkworm cocoons. Despite their different origins and sequence varieties many of these fibrous proteins share a common building principle: they consist of a large repetitive core domain flanked by relatively small non-repetitive terminal domains. Amongst protein fibers, spider dragline silk shows prominent mechanical properties that exceed those of man-made fibers like Kevlar. Spider silk fibers assemble in a spinning process allowing the transformation from an aqueous solution into a solid fiber within milliseconds. Here, we highlight the role of the non-repetitive terminal domains of spider dragline silk proteins during storage in the gland and initiation of the fiber assembly process. (C) 2011 Wiley Periodicals, Inc. Biopolymers 97: 355361, 2012.

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