Spider silk and amyloid fibrils: a structural comparison

Macromol Biosci. 2007 Feb 12;7(2):183-8. doi: 10.1002/mabi.200600201.


Although spider silks have been studied for decades, the assembly properties of the underlying silk proteins have still not been unravelled. Previously, the detection of amyloid-like nanofibrils in the spider's silk gland suggested their involvement in the assembly process.Recombinantly produced spider silk also self-assembles into nanofibrils. In order to investigate the structural properties of such silk nanofibrils in more detail, they have been compared to amyloid-like fibrils to highlight structural similarities.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amyloid / chemistry*
  • Animals
  • Benzothiazoles
  • Circular Dichroism
  • Congo Red
  • Fungal Proteins / chemistry*
  • Microscopy, Atomic Force
  • Peptide Termination Factors
  • Prions / chemistry*
  • Saccharomyces cerevisiae Proteins / chemistry*
  • Silk / chemistry*
  • Spectroscopy, Fourier Transform Infrared
  • Spiders / chemistry*
  • Thiazoles / metabolism
  • X-Ray Diffraction


  • Amyloid
  • Benzothiazoles
  • Fungal Proteins
  • Peptide Termination Factors
  • Prions
  • SUP35 protein, S cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Silk
  • Thiazoles
  • thioflavin T
  • Congo Red