The aggregation and membrane-binding properties of an α-synuclein peptide fragment

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

    Research output: Contribution to journalArticlepeer-review


    α-Synuclein is a 140 amino acid protein, which is associated with presynaptic membranes in the brain, and is the major component of protein aggregates produced during the progression of many neurodegenerative diseases. It has been shown that a central hydrophobic region of α-synuclein comprising residues 71-82 is required for aggregation of the protein into the fibrillar form found in pathogenic aggregates [Giasson, Murray, Trojanowski and Lee (2001) J. Biol. Chem. 276, 2380-2386]. In the present study, we used 2H NMR and electron microscopy to investigate the aggregation and membrane-binding properties of a synthetic peptide corresponding to this region. Results indicate that this region associates with phospholipid bilayers but also forms amyloid-like fibrils in the absence of lipid membranes.
    Original languageEnglish
    Pages (from-to)1127-1129
    Number of pages2
    JournalBiochemical Society Transactions
    Issue number6
    Publication statusPublished - Dec 2004


    • α-synuclein
    • Aggregation
    • Electron microscopy
    • Membrane binding
    • Neurodegenerative diseases
    • NMR


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