Amyloids: friend or foe?

J Alzheimers Dis. 2008 May;13(4):407-19. doi: 10.3233/jad-2008-13406.


Amyloidogenesis is the aggregation of soluble proteins into structurally conserved fibers. Amyloid fibers are distinguished by their resistance to proteinase K, tinctorial properties and beta-sheet-rich secondary structure. Amyloid formation is a hallmark of many human diseases including Alzheimer's, Huntington's and the prion diseases. Therefore, understanding amyloidogenesis will provide insights into the development of therapeutics that target these debilitating diseases. A new class of ;functional' amyloids promises a unique glimpse at how nature has harnessed the amyloid fiber to accomplish important physiological tasks. Functional amyloids are produced by organisms spanning all aspects of cellular life. Herein we review amyloidogenesis, with special attention focused on the similarities and differences between the best characterized disease-associated amyloidogenic protein amyloid-beta and the formation of several functional amyloids. The implications of studying functional amyloidogenesis and the strategies organisms employ to limit exposure to toxic intermediates will also be discussed.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Amyloid / metabolism
  • Amyloid / physiology*
  • Anti-Bacterial Agents / therapeutic use
  • Bacterial Proteins / metabolism
  • Bacteriocins / therapeutic use
  • Escherichia coli Proteins / metabolism
  • Humans
  • Membrane Glycoproteins / metabolism
  • Neurodegenerative Diseases / drug therapy
  • Neurodegenerative Diseases / metabolism
  • Neurodegenerative Diseases / microbiology
  • gp100 Melanoma Antigen


  • Amyloid
  • Anti-Bacterial Agents
  • Bacterial Proteins
  • Bacteriocins
  • Escherichia coli Proteins
  • Membrane Glycoproteins
  • PMEL protein, human
  • csgA protein, E coli
  • gp100 Melanoma Antigen
  • microcin
  • Crl protein, Bacteria