Neuronal and oligodendrocytic aggregates of fibrillar α-synuclein define several diseases of
the nervous system. It is likely that these inclusions impair vital metabolic processes and
compromise vialibity of affected cells. Here, we report that a 12-amino acid stretch (71
VTGVTAVAQKTV 82) in the middle of the hydrophobic domain of human α-synuclein is
necessary and sufficient for its fibrillization based on the following observations: 1) human β-
synuclein is highly homologous to α-synuclein but lacks these 12 residues, and it does not …