The role of salt and shear on the storage and assembly of spider silk proteins

Lukas Eisoldt, John G. Hardy, Markus Heim, Thomas R. Scheibel*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

62 Citations (Scopus)
477 Downloads (Pure)

Abstract

Major ampullate silk fibers of orb web-weaving spiders have impressive mechanical properties due to the fact that the underlying proteins partially fold into helical/amorphous structures, yielding relatively elastic matrices that are toughened by anisotropic nanoparticulate inclusions (formed from stacks of beta-sheets of the same proteins). In vivo the transition from soluble protein to solid fibers involves a combination of chemical and mechanical stimuli (such as ion exchange, extraction of water and shear forces). Here we elucidate the effects of such stimuli on the in vitro aggregation of engineered and recombinantly produced major ampullate silk-like proteins (focusing on structure-function relationships with respect to their primary structures), and discuss their relevance to the storage and assembly of spider silk proteins in vivo. (C) 2009 Elsevier Inc. All rights reserved.

Original languageEnglish
Pages (from-to)413-419
Number of pages7
JournalJournal of structural biology
Volume170
Issue number2
Early online date04 Jan 2010
DOIs
Publication statusPublished - May 2010

Keywords

  • Spider silk
  • Protein assembly
  • Salt
  • Shear
  • MAJOR AMPULLATE GLAND
  • C-TERMINAL DOMAIN
  • FIBER FORMATION
  • HOFMEISTER SERIES
  • DRAGLINE
  • CONFORMATION
  • ORIENTATION
  • MECHANISM
  • INSECTS
  • FIBROIN

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Biomaterials

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