The deposition of α-syn (α-synuclein) fibrils in Lewy bodies is a characteristic feature of individuals with neurodegenerative disorders. A peptide comprising the central residues 71–82 of α-syn [α-syn(71–82)] is capable of forming β-sheet-rich, amyloid-like fibrils with similar morphologies to fibrils of the full-length protein, providing a useful model of pathogenic α-syn fibrils that is suitable for detailed structural analysis. We have studied the morphology and gross structural features of α-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.
Research Article| October 26 2005
Studies of the aggregation of an amyloidogenic α-synuclein peptide fragment
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J. Madine, A.J. Doig, A. Kitmitto, D.A. Middleton; Studies of the aggregation of an amyloidogenic α-synuclein peptide fragment. Biochem Soc Trans 26 October 2005; 33 (5): 1113–1115. doi: https://doi.org/10.1042/BST0331113
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