Ubiquitous amyloids

Appl Biochem Biotechnol. 2012 Apr;166(7):1626-43. doi: 10.1007/s12010-012-9549-3. Epub 2012 Feb 19.

Abstract

The common view of amyloids and prion proteins is that they are associated with many currently incurable diseases and present a great danger to an organism. This danger comes from the fact that not only prion proteins, but also the infectious form(s) of amyloids, as it has been shown recently, are able to transmit the disease. On the other hand, organisms take advantage of the strength and durability of specific forms of amyloids. Such forms do not spread any disease. Also, in nanotechnology there is a constantly growing need to employ amyloid fibrils in many industrial applications. With increasing knowledge about amyloids and prion proteins we are aware that the amyloidal state is inherent to any protein, making the problem of amyloid formation a central one in aging-related diseases. However, the "good" amyloids can be beneficial and even necessary for our health. Furthermore, because of their mechanical properties, the amyloids are of great interest to engineers.

Publication types

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

MeSH terms

  • Aging*
  • Amino Acid Motifs
  • Amyloid / chemistry*
  • Amyloid / metabolism
  • Amyloid beta-Peptides / chemistry*
  • Amyloid beta-Peptides / metabolism
  • Chemical Engineering
  • Computer Simulation
  • Humans
  • Hydrogen Bonding
  • Models, Molecular
  • Prions / chemistry*
  • Prions / metabolism
  • Protein Denaturation
  • Protein Structure, Secondary

Substances

  • Amyloid
  • Amyloid beta-Peptides
  • Prions