Methionine oxidation inhibits fibrillation of human α-synuclein in vitro

被引：186

作者：

Uversky, VN ^{[1
]}

Yamin, G

Souillac, PO

Goers, J

Glaser, CB

Fink, AL

机构：

[1] Univ Calif Santa Cruz, Dept Chem & Biochem, Santa Cruz, CA 95064 USA

[2] Russian Acad Sci, Inst Biol Instrumentat, Pushchino 142292, Moscow Region, Russia

[3] Calif Polytech State Univ San Luis Obispo, San Luis Obispo, CA 93407 USA

来源：

FEBS LETTERS | 2002年 / 517卷 / 1-3期

基金：

美国国家卫生研究院;

关键词：

Parkinson's disease; alpha-synuclein; oxidative stress; methionine oxidation; fibrillation; inhibition of fibrillation; partially folded intermediate;

D O I：

10.1016/S0014-5793(02)02638-8

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

We examined the effect of methionine oxidation of human recombinant alpha-synuclein on its structural properties and propensity to fibrillate. Both oxidized and non-oxidized alpha-synucleins were natively unfolded under conditions of neutral pH, with the oxidized protein being slightly more disordered. Both proteins adopted identical partially folded conformations under conditions of acidic pH. The fibrillation of alpha-synuclein at neutral pH was completely inhibited by methionine oxidation. This inhibitory effect was eliminated at low pH. The addition of oxidized alpha-synuclein to the unoxidized form led to a substantial inhibition of alpha-synuclein fibrillation. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

引用

页码：239 / 244

页数：6

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