Amyloid β Protein: Aβ40 Inhibits Aβ42 Oligomerization

被引：99

作者：

Murray, Megan M. ^{[1
]}

Bernstein, Summer L. ^{[1
]}

Nyugen, Vy ^{[1
]}

Condron, Margaret M. ^{[2
,3
,4
]}

Teplow, David B. ^{[2
,3
,4
]}

Bowers, Michael T. ^{[1
]}

机构：

[1] Univ Calif Santa Barbara, Dept Chem & Biochem, Santa Barbara, CA 93106 USA

[2] Univ Calif Los Angeles, Inst Mol Biol, Los Angeles, CA 90095 USA

[3] Univ Calif Los Angeles, Dept Neurol, David Geffen Sch Med, Los Angeles, CA 90095 USA

[4] Univ Calif Los Angeles, Brain Res Inst, Los Angeles, CA 90095 USA

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2009年 / 131卷 / 18期

基金：

美国国家卫生研究院;

关键词：

MONOMER STRUCTURE; AGGREGATION;

D O I：

10.1021/ja8092604

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

A beta 40 and A beta 42 are peptides that adopt similar random-coil structures in solution. A beta 42, however, is significantly more neurotoxic than A beta 40 and forms amyloid fibrils much more rapidly than A beta 40. Here, mass spectrometry and ion mobility spectrometry are used to investigate a mixture of A beta 40 and A beta 42. The mass spectrum for the mixed solution shows the presence of a heterooligomer composed of equal parts of A beta 40 and A beta 42. Ion mobility results indicate that this mixed species comprises an oligomer distribution extending to tetramers. A beta 40 atone produces such a distribution, whereas A beta 42 alone produces oligomers as large as dodecamers. This indicates that A beta 40 inhibits A beta 42 oligomerization.

引用

页码：6316 / +

页数：3

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