Dopamine promotes α‐synuclein aggregation into SDS‐resistant soluble oligomers via a distinct folding pathway

Abstract

ABSTRACT Dopamine (DA) and α‐synuclein (α‐SN) are two key molecules associated with Parkinson's disease (PD). We have identified a novel action of DA in the initial phase of α‐SN aggregation and demonstrate that DA induces α‐SN to form soluble, SDS‐resistant oligomers. The DA:α‐SN oligomeric species are not amyloidogenic as they do not react with thioflavin T and lack the typical amyloid fibril structures as visualized with electron microscopy. Circular dichroism studies indicate that in the presence of lipid membranes DA interacts with α‐SN, causing an alteration to the structure of the protein. Furthermore, DA inhibited the formation of iron‐induced α‐SN amyloidogenic agg..