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Coordination of platinum to α-synuclein inhibits filamentous aggregation in solution.

Accumulation of filamentous aggregates of α-synuclein (AS) in Lewy bodies and neurites characterizes neurodegenerative diseases such as Parkinson's disease. Inhibition of AS fibrillation is helpful for understanding of AS aggregate structure and for developing chemical therapies. Herein we report that the Pt(II)-containing antitumor drug cisplatin suppresses filamentous aggregation of AS in solution. Pt(II) contrasts strongly with reported transition-metal ions such as Mn(II), Fe(III), and Cu(II), which accelerate AS aggregation. Interaction of Pt(II) with sidechains of methionine and histidine residues was essential for inhibition of AS fibrillation. Binding of Pt(II) to AS did not change the polypeptide's overall random coil structure, as indicated by solution-state two-dimensional NMR and circular dichroism spectroscopy; and a solution of the AS-Pt(II) complex remained free of filamentous aggregates. Our results constitute interesting new information about the biological chemistry of metal ions in Parkinson's disease and may open new lines of research on the suppression of the filamentous aggregation.

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