Journal article

The N-Terminal Residues 43 to 60 Form the Interface for Dopamine Mediated alpha-Synuclein Dimerisation

Su Ling Leong, Mark G Hinds, Andrea R Connor, David P Smith, Eva Illes-Toth, Chi LL Pham, Kevin J Barnham, Roberto Cappai

PLOS ONE | PUBLIC LIBRARY SCIENCE | Published : 2015

Abstract

α-synuclein (α-syn) is a major component of the intracellular inclusions called Lewy bodies, which are a key pathological feature in the brains of Parkinson's disease patients. The neurotransmitter dopamine (DA) inhibits the fibrillisation of α-syn into amyloid, and promotes α-syn aggregation into SDS-stable soluble oligomers. While this inhibition of amyloid formation requires the oxidation of both DA and the methionines in α-syn, the molecular basis for these processes is still unclear. This study sought to define the protein sequences required for the generation of oligomers. We tested N- (α-syn residues 43-140) and C-terminally (1-95) truncated α-syn, and found that similar to full-lengt..

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