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Papers In Press, published online ahead of print August 26, 2002
Department of Chemistry, Case Western Reserve University, Cleveland, OH 44139-7078
Corresponding Author: mxz12{at}po.cwru.edu
The major component of amyloid plaques in Alzheimer’s disease (AD) is the Abeta, a small peptide that has high propensity to assemble as aggregated beta-sheet structures. Using three well established techniques for studying amyloid structure, namely circular dichroism, thioflavin-T fluorescence, and atomic force microscopy, we demonstrate that oxidation of the methionine-35 (Met35) side chain to a methionine sulfoxide (Met35ox) significantly hinders the rate of fibril formation for the 42-residue Abeta(1-42) in solution at physiological pH. The Met35ox also alters the characteristic Abeta fibril morphology and prevents formation of the protofibril, which is a key intermediate in beta-amyloidosis and the associated neurotoxicity. The implications of these results to the biological function and role of the Abeta with oxidative stress in AD are discussed.
J. Biol. Chem, 10.1074/jbc.C200338200
Submitted on June 3, 2002
Revised on August 14, 2002
Accepted on August 26, 2002
Methionine-32 oxidation reduces fibril assembly of the amyloid Abeta(1-42) peptide of Alzheimer's disease
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