Abstract
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.
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