Specific chaperones and regulatory domains in control of amyloid formation

J Biol Chem. 2015 Oct 30;290(44):26430-6. doi: 10.1074/jbc.R115.653097. Epub 2015 Sep 9.


Many proteins can form amyloid-like fibrils in vitro, but only about 30 amyloids are linked to disease, whereas some proteins form physiological amyloid-like assemblies. This raises questions of how the formation of toxic protein species during amyloidogenesis is prevented or contained in vivo. Intrinsic chaperoning or regulatory factors can control the aggregation in different protein systems, thereby preventing unwanted aggregation and enabling the biological use of amyloidogenic proteins. The molecular actions of these chaperones and regulators provide clues to the prevention of amyloid disease, as well as to the harnessing of amyloidogenic proteins in medicine and biotechnology.

Keywords: BRICHOS; lung surfactant; molecular chaperone; pH regulation; prion; protein domain; protein structure; spider silk protein.

Publication types

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

MeSH terms

  • Amyloid / metabolism*
  • Animals
  • Humans
  • Molecular Chaperones / metabolism*


  • Amyloid
  • Molecular Chaperones