α-Synuclein (α-Syn) is a 140-amino acid protein, which is encoded by the gene SNCA. α-Syn was first isolated from the cholinergic neurons of Torpedo californica. The protein localizes only to synaptic vesicles and portions of the nucleus, hence the name synuclein. Three additional synuclein family members have been identified and are named β-syn, γ-syn, and synoretnin. Only α- and β-syn are expressed in the mammalian brain[1]. α-Syn is a typical intrinsically disordered protein, but can adopt a number of different conformational states depending on conditions and cofactors. These include the helical membrane-bound form, a partially-folded state that is a key intermediate in aggregation and fibrillation, various oligomeric species, and fibrillar and amorphous aggregates.Although the normal function (or functions) of α-syn remains unknown, its localization at presynaptic terminals, its association with the distal reserve pool of synaptic vesicles and the deficiencies in synaptic transmissions observed in response to knockdown or overexpression of α-syn suggest that α-syn has a role in the regulation of neurotransmitter release, synaptic function and plasticity[2]. Human genetics has indicated a causal role for the protein α-synuclein in the pathogenesis of familial Parkinson’s disease (PD). In both sporadic and dominant familial forms of PD and related neurodegenerative disorders α-Syn is misfolded and deposited within insoluble protein aggregates, which are robustly expressed within Lewy bodies (LBs). This accumulation of misfolded α-synuclein is widely recognized as a hallmark of multiple forms of neural degeneration[3],[4].