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

J Struct Biol. 2010 May;170(2):413-9. doi: 10.1016/j.jsb.2009.12.027. Epub 2010 Jan 4.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Materials Testing
  • Molecular Sequence Data
  • Protein Conformation*
  • Protein Folding
  • Recombinant Fusion Proteins / chemistry
  • Recombinant Fusion Proteins / genetics
  • Salts / chemistry*
  • Shear Strength
  • Silk / chemistry*
  • Silk / genetics
  • Spectroscopy, Fourier Transform Infrared
  • Spiders / anatomy & histology
  • Spiders / chemistry*
  • Stress, Mechanical


  • Recombinant Fusion Proteins
  • Salts
  • Silk