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Originally published In Press as doi:10.1074/jbc.C200338200 on August 26, 2002

J. Biol. Chem., Vol. 277, Issue 43, 40173-40176, October 25, 2002
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ACCELERATED PUBLICATION
Methionine 35 Oxidation Reduces Fibril Assembly of the Amyloid Abeta -(1-42) Peptide of Alzheimer's Disease*

Liming HouDagger , Inkyung Kang§, Roger E. Marchant§, and Michael G. ZagorskiDagger

From the Departments of Dagger  Chemistry and § Biomedical Engineering, Case Western Reserve University, Cleveland, Ohio 44106-7078

The major component of amyloid plaques in Alzheimer's disease (AD) is 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 Met-35 side chain to a methionine sulfoxide (Met-35ox) significantly hinders the rate of fibril formation for the 42-residue Abeta -(1-42) at physiological pH. Met-35ox 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 for the biological function and role of Abeta with oxidative stress in AD are discussed.

* This work was supported in part by grants from the National Institutes of Health (AG-14363-04 to M. G. Z.; HL-40047-12, HL-47300-05, and HL-70263-01 to R. E. M.) and the American Health Assistance Foundation (A2000-056 to M. G. Z.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Dept. of Chemistry, Case Western Reserve University, Cleveland, OH 44106-7078. Tel.: 216-368-3706; Fax: 216-368-3006; E-mail: mxz12@po.cwru.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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Copyright © 2002 by the American Society for Biochemistry and Molecular Biology.