Studies of the aggregation of an amyloidogenic α-synuclein peptide fragment

J. Madine, A. J. Doig, A. Kitmitto, D. A. Middleton

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    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. ©2005 Biochemical Society.
    Original languageEnglish
    Pages (from-to)1113-1115
    Number of pages2
    JournalBiochemical Society Transactions
    Issue number5
    Publication statusPublished - Nov 2005


    • α-synuclein
    • Aggregation
    • Circular dichroism (CD)
    • Electron microscopy (EM)
    • Fibril morphology
    • Neurodegenerative disease


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