α-Synuclein (61-75) is a peptide fragment derived from the larger protein α-Synuclein, which is predominantly found in presynaptic nerve terminals and considered a biomarker candidate for Parkinson's disease (PD).

Lewy bodies containing α-Synuclein are key neuropathological indicators of Parkinson's Disease (PD). Mutations in α-Synuclein (A30P, E46K, H50Q, G51D, A53E, A53T), along with gene duplications and triplications, directly cause PD. Polymorphisms in α-Synuclein gene regulatory elements also increase susceptibility to PD and are linked to early onset. The non-Aβ-amyloid component (NAC) of α-Synuclein is hydrophobic and prone to aggregation, unlike its counterparts in mice and human β-Synuclein, which do not aggregate. β-Synuclein shares greater homology with α-Synuclein in the N-terminal sequences (74%) compared to γ-Synuclein (67%)[1].