β-Synuclein is a presynaptic protein that plays an important role in neuronal plasticity and synaptic vesicle regulation. The synuclein family includes three members: α, β and γ isoforms. The presynaptic proteins are detected in the neocortex, hippocampus, striatum, thalamus, and cerebellum regions^1,2. β-Synuclein has been shown to act as a negative regulator of α-synuclein aggregation both in vivo and in vitro^1,2. Structure wise, the protein contains a highly conserved N-terminal domain which includes a repetitive amino acid motif, and a more divergent and highly acidic stretch at the C-terminal domain^2,3.

Studies have shown overexpressed mRNA levels of β-synuclein in Parkinson's disease suggesting that the protein has a valuable role in maintaining homeostasis in the disease pathology. In addition, studies have shown the action of β-synuclein as a neurodegeneration-inducing factor that can cause cell loss when expressed in rat brains^1,2.

β-Synuclein is also implicated with dementia involving Lewy bodies. To date, two mutations in the protein, V70M and P123H, have been identified in the sporadic and familial disease³.