Mass Spectrometry and the Amyloid Problem-How Far Can We Go in the Gas Phase?

被引：58

作者：

Ashcroft, Alison E. ^{[1
]}

机构：

[1] Univ Leeds, Inst Mol & Cellular Biol, Astbury Ctr Struct Mol Biol, Leeds LS2 9JT, W Yorkshire, England

来源：

JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY | 2010年 / 21卷 / 07期

基金：

英国惠康基金; 英国生物技术与生命科学研究理事会;

关键词：

ION MOBILITY MEASUREMENTS; HYDROGEN-EXCHANGE; FIBRIL FORMATION; HYDROGEN/DEUTERIUM EXCHANGE; ALZHEIMERS-DISEASE; BETA-PEPTIDE; IN-VITRO; PROTEIN AGGREGATION; LIMITED PROTEOLYSIS; MISFOLDING DISEASES;

D O I：

10.1016/j.jasms.2010.02.026

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

A number of proteins are capable of converting from their soluble, monomeric form into highly-ordered, insoluble aggregates known as amyloid fibrils. In vivo, these fibrils, which accumulate in organs and tissues, are associated with a wide range of amyloid diseases for which there are currently no therapeutic solutions. The molecular details of the pathway from native monomer through oligomeric intermediates to the final amyloid fibril remain a challenging enigma. Over the past few years, mass spectrometry has been applied to investigate the various stages of amyloid fibril formation, and this report summarizes the key steps achieved to date. (J Am Soc Mass Spectrom 2010, 21, 1087-1096) (C) 2010 American Society for Mass Spectrometry

引用

收藏

页码：1087 / 1096

页数：10

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