Annual Review of Analytical Chemistry ( IF 5.9 ) Pub Date : 2017-06-12 00:00:00 , DOI: 10.1146/annurev-anchem-071114-040304 Christian Bleiholder 1 , Michael T. Bowers 2
Ion mobility spectrometry-mass spectrometry (IMS-MS) methods are increasingly used to study noncovalent assemblies of peptides and proteins. This review focuses on the noncovalent self-assembly of amino acids and peptides, systems at the heart of the amyloid process that play a central role in a number of devastating diseases. Three different systems are discussed in detail: the 42-residue peptide amyloid-β42 implicated in the etiology of Alzheimer's disease, several amyloid-forming peptides with 6–11 residues, and the assembly of individual amino acids. We also discuss from a more fundamental perspective the processes that determine how quickly proteins and their assemblies denature when the analyte ion has been stripped of its solvent in an IMS-MS measurement and how to soften the measurement so that biologically meaningful data can be recorded.
中文翻译:
使用离子迁移方法的生物分子溶液组装:从氨基酸到淀粉样β蛋白
离子淌度质谱-质谱(IMS-MS)方法越来越多地用于研究肽和蛋白质的非共价组装。这篇综述着重于氨基酸和肽的非共价自组装,这是淀粉样蛋白过程的核心系统,在许多毁灭性疾病中起着核心作用。详细讨论了三种不同的系统:与阿尔茨海默氏病的病因有关的42个残基的淀粉样蛋白β42,几个具有6-11个残基的淀粉样蛋白形成肽以及单个氨基酸的组装。