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流动辅助离子迁移质谱(FAIMS)在蛋白质分析中具有多大的益处?

To What Extent is FAIMS Beneficial in the Analysis of Proteins?

作者信息

Cooper Helen J

机构信息

School of Biosciences, University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK.

出版信息

J Am Soc Mass Spectrom. 2016 Apr;27(4):566-77. doi: 10.1007/s13361-015-1326-4. Epub 2016 Feb 2.

Abstract

High field asymmetric waveform ion mobility spectrometry (FAIMS), also known as differential ion mobility spectrometry, is emerging as a tool for biomolecular analysis. In this article, the benefits and limitations of FAIMS for protein analysis are discussed. The principles and mechanisms of FAIMS separation of ions are described, and the differences between FAIMS and conventional ion mobility spectrometry are detailed. Protein analysis is considered from both the top-down (intact proteins) and the bottom-up (proteolytic peptides) perspective. The roles of FAIMS in the analysis of complex mixtures of multiple intact proteins and in the analysis of multiple conformers of a single protein are assessed. Similarly, the application of FAIMS in proteomics and targeted analysis of peptides are considered.

摘要

高场不对称波形离子迁移谱(FAIMS),也称为差分离子迁移谱,正逐渐成为一种用于生物分子分析的工具。本文讨论了FAIMS用于蛋白质分析的优点和局限性。描述了FAIMS分离离子的原理和机制,并详细阐述了FAIMS与传统离子迁移谱之间的差异。从自上而下(完整蛋白质)和自下而上(蛋白水解肽)两个角度对蛋白质分析进行了探讨。评估了FAIMS在多种完整蛋白质复杂混合物分析以及单一蛋白质多种构象分析中的作用。同样,也考虑了FAIMS在蛋白质组学和肽段靶向分析中的应用。

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