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.
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November 2004
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Conference Article|
October 26 2004
The aggregation and membrane-binding properties of an α-synuclein peptide fragment
J. Madine;
J. Madine
1Department of Biomolecular Sciences, UMIST, P.O. Box 88, Sackville Street, Manchester M60 1QD, U.K.
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A.J. Doig;
A.J. Doig
1Department of Biomolecular Sciences, UMIST, P.O. Box 88, Sackville Street, Manchester M60 1QD, U.K.
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D.A. Middleton
D.A. Middleton
1
1Department of Biomolecular Sciences, UMIST, P.O. Box 88, Sackville Street, Manchester M60 1QD, U.K.
1To whom correspondence should be addressed (email david.a.middleton@umist.ac.uk).
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Biochem Soc Trans (2004) 32 (6): 1127–1129.
Article history
Received:
July 02 2004
Citation
J. Madine, A.J. Doig, D.A. Middleton; The aggregation and membrane-binding properties of an α-synuclein peptide fragment. Biochem Soc Trans 1 November 2004; 32 (6): 1127–1129. doi: https://doi.org/10.1042/BST0321127
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