In situ analysis of intact proteins by ion mobility mass spectrometry
In situ analysis of intact proteins by ion mobility mass spectrometry
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DOI：
10.1016/j.trac.2019.05.036
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发表时间：
2020-03
期刊：
影响因子：
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通讯作者：
Emma K Sisley;Eva Illes-Toth;H. Cooper
中科院分区：
文献类型：
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作者：
Emma K Sisley;Eva Illes-Toth;H. Cooper
我们描述了离子迁移质谱技术用于完整蛋白质的状态分析，即直接从其生物环境中分析蛋白质。原位分析的好处包括与完整蛋白质分析更广泛相关的好处，例如，保留翻译后修饰和直接确定氨基酸取代之间的连通性，以及与表面采样相关的好处，例如，保留空间信息。采样技术包括液体萃取表面分析，连续流动液体-微结表面采样，解吸电喷雾电离和基质辅助激光解吸/电离。直接表面采样受到固有样品复杂性的挑战，这一挑战可以通过离子迁移谱法的集成来解决。目前，行波离子迁移率光谱法和高场不对称波形离子迁移率光谱法已被应用于蛋白质的原位分析领域。在行波离子迁移率光谱法的情况下，还可以获得与三级或四级结构有关的信息。
We describe ion mobility mass spectrometry techniques for thein situanalysis of intact proteins, i.e., the analysis of proteins directly from their biological environment. The benefits ofin situanalysis include those associated more broadly with analysis of intact proteins, e.g., retention of connectivity between post-translational modifications and direct determination of amino acid substitutions, and those associated with surface sampling, e.g., retention of spatial information. Sampling techniques include liquid extraction surface analysis, continuous-flow liquid-microjunction surface sampling, desorption electrospray ionisation and matrix assisted laser desorption/ionisation. Direct surface sampling is beset by the challenge of inherent sample complexity, a challenge which can be addressed through integration of ion mobility spectrometry. To date, travelling wave ion mobility spectrometry and high field asymmetric waveform ion mobility spectrometry have been applied to the area ofin situanalysis of proteins. In the case of travelling wave ion mobility spectrometry, information relating to tertiary or quaternary structure can also be obtained.