Studies of an early stage amyloid formation for Parkinson`s Disease casual protein.

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In this study, we have focused on α-synuclein, the major component of amyloid plaque in Parkinson's Disease (PD). The relationship between a detailed mechanism of amyloid formations and PD has been investigated. In particular, an interaction between α-synuclein and dopamine, a neurotransmitter and well known treatment for PD, has been elucidated in terms of its effect on amyloid formation, using fluorescence, CD, gelfilteration chromatography, NMR and MS. As a result, we have shown that the presence of dopamine suppresses the formation of amyloid fibrils, while theformation of oligomer intermediates is stabilized by addition of dopamine. Furthermore, the complex formation between α-synuclein and dopamine has been confirmed, with a binding ratio of 1 to 3 dopamine molecules per α-synuclein molecule. In conclusion, we have proposed a schematic model for the mechanism of α-synuclein oligomer intermediates and amyloid formations.