Beta-synuclein exhibits chaperone activity more efficiently than alpha-synuclein

FEBS Lett. 2004 Oct 8;576(1-2):256-60. doi: 10.1016/j.febslet.2004.08.075.


Beta-synuclein exhibits high sequence homology and structural similarity with alpha-synuclein, a protein implicated in the pathogenesis of Parkinson's disease. We investigated the chaperone function of beta-synuclein and its anti-fibrillar activity in comparison with alpha-synuclein. beta-Synuclein suppressed the heat-induced aggregation of aldolase, alcohol dehydrogenase, and citrate synthase, and its anti-aggregative activity was remarkably higher than that of alpha-synuclein. Heat-induced inactivation of citrate synthase was significantly protected by beta-synuclein. Moreover, beta-synuclein inhibited the amyloid formation of both Abeta(1-40) and alpha-synuclein. It is, therefore, suggested that beta-synuclein can prevent abnormal protein aggregations more effectively than alpha-synuclein by acting as a molecular chaperone.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Amyloid beta-Peptides / antagonists & inhibitors
  • Citrate (si)-Synthase / metabolism
  • Hot Temperature
  • Molecular Chaperones*
  • Molecular Sequence Data
  • Nerve Tissue Proteins / chemistry
  • Nerve Tissue Proteins / metabolism*
  • Sequence Homology, Amino Acid
  • Synucleins
  • alpha-Synuclein
  • beta-Synuclein


  • Amyloid beta-Peptides
  • Molecular Chaperones
  • Nerve Tissue Proteins
  • Synucleins
  • alpha-Synuclein
  • beta-Synuclein
  • Citrate (si)-Synthase