β-Synuclein exhibits high sequence homology and structural similarity with α-synuclein, a protein implicated in the pathogenesis of Parkinson's disease. We investigated the chaperone function of β-synuclein and its anti-fibrillar activity in comparison with α-synuclein. β-Synuclein suppressed the heat-induced aggregation of aldolase, alcohol dehydrogenase, and citrate synthase, and its anti-aggregative activity was remarkably higher than that of α-synuclein. Heat-induced inactivation of citrate synthase was significantly protected by β-synuclein. Moreover, β-synuclein inhibited the amyloid formation of both Aβ 1-40 and α-synuclein. It is, therefore, suggested that β-synuclein can prevent abnormal protein aggregations more effectively than α-synuclein by acting as a molecular chaperone. © 2004 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
Lee, D., Paik, S. R., & Choi, K. Y. (2004). β-Synuclein exhibits chaperone activity more efficiently than α-synuclein. FEBS Letters, 576(1–2), 256–260. https://doi.org/10.1016/j.febslet.2004.08.075