The deposition of alpha-syn (alpha-synuclein) fibrils in Lewy bodies is a characteristic feature of individuals with neurodegenerative disorders. A peptide comprising the central residues 71-82 of alpha-syn [alpha-syn(71-82)] is capable of forming beta-sheet-rich, amyloid-like fibrils with similar morphologies to fibrils of the full-length protein, providing a useful model of pathogenic alpha-syn fibrils that is suitable for detailed structural analysis. We have studied the morphology and gross structural features of alpha-syn(71-82) fibrils formed under different conditions in order to obtain reliable conditions for producing fibrils for further structural investigations. The results indicate that the rate of aggregation and the morphology of the fibrils formed are sensitive to pH and temperature.