基于质谱的蛋白质组学的高场非对称波形离子迁移谱。
High-field asymmetric waveform ion mobility spectrometry for mass spectrometry-based proteomics.
机构信息
Institute for Systems Biology, 401 Terry Avenue N, Seattle, WA 98109, USA.
出版信息
Expert Rev Proteomics. 2012 Oct;9(5):505-17. doi: 10.1586/epr.12.50.
Abstract
High-field asymmetric waveform ion mobility spectrometry (FAIMS) is an atmospheric pressure ion mobility technique that separates gas-phase ions by their behavior in strong and weak electric fields. FAIMS is easily interfaced with electrospray ionization and has been implemented as an additional separation mode between liquid chromatography (LC) and mass spectrometry (MS) in proteomic studies. FAIMS separation is orthogonal to both LC and MS and is used as a means of on-line fractionation to improve the detection of peptides in complex samples. FAIMS improves dynamic range and concomitantly the detection limits of ions by filtering out chemical noise. FAIMS can also be used to remove interfering ion species and to select peptide charge states optimal for identification by tandem MS. Here, the authors review recent developments in LC-FAIMS-MS and its application to MS-based proteomics.
摘要
高场非对称波形离子淌度谱（FAIMS）是一种大气压离子淌度技术，通过在强电场和弱电场中的行为来分离气相离子。FAIMS 易于与电喷雾电离接口，并且已经作为在蛋白质组学研究中在液相色谱（LC）和质谱（MS）之间的附加分离模式被实现。FAIMS 分离与 LC 和 MS 均正交，并作为在线分馏的手段用于改善复杂样品中的肽的检测。FAIMS 通过过滤化学噪声来改善离子的动态范围并同时提高检测限。FAIMS 还可用于去除干扰离子物种，并选择用于串联 MS 鉴定的最佳肽电荷状态。在这里，作者综述了 LC-FAIMS-MS 的最新进展及其在基于 MS 的蛋白质组学中的应用。
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