Parkinson's disease is predominantly a movement disorder resulting from degeneration of dopaminergic neurons in the substantia nigra. The cause of the disease is unknown, but substantial evidence suggests that the aggregation of α-synuclein is a critical step in the etiology of Parkinson's disease (PD). α-Synuclein is an abundant brain protein of 140 residues that is present in high concentration at presynaptic terminals and is found in both soluble and membrane-associated fractions of the brain. Several possible functions have been suggested for α-synuclein, and it also appears to be involved in vesicle release and trafficking. In vitro incubation in the presence of a specific amount of salt (i.e. 0.1M NaCl) with agitation shows α-synuclein forming fibrilous structure.
Recombinant human α-synuclein (1-140) (GenBank Accession # NP_000336) was expressed and purified from E. coli and conjugated with biotin.