Dopamine quinones interact with α-synuclein to form unstructured adducts

摘要: Abstract α-Synuclein (αsyn) fibril formation is considered a central event in the pathogenesis of Parkinson’s disease (PD). In recent years, it has been proposed that prefibrillar annular oligomeric β-sheet-rich species, called protofibrils, rather than fibrils themselves, may be neurotoxic species. The oxidation products dopamine (DAQ) can inhibit αsyn supporting idea DAQ might stabilize protofibrils. present work, through different biochemical and biophysical techniques, we isolated structurally characterized αsyn/DAQ adducts. Contrary to demonstrated adducts retain an unfolded conformation. We then investigated nature modifications induced on by DAQ. Our results indicate only small fraction interacts with covalent way, so non-covalent interaction appears major modification αsyn.