High-field asymmetric waveform ion mobility spectrometry for mass spectrometry-based proteomics.
High-field asymmetric waveform ion mobility spectrometry for mass spectrometry-based proteomics.
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DOI：
10.1586/epr.12.50
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发表时间：
2012-10
影响因子：
3.4
通讯作者：
Moritz RL
中科院分区：
文献类型：
--
作者：
Swearingen KE;Moritz RL
高场非对称波形离子迁移谱（FAIMS）是一种大气压下的离子迁移技术，它利用气相离子在强电场和弱电场中的行为来分离气相离子。FAIMS很容易与电喷雾离子化连接，并已在蛋白质组学研究中作为液相色谱（LC）和质谱（MS）之间的附加分离模式。FAIMS分离与LC和MS均正交，并用作在线分馏的手段，以改善复杂样品中肽的检测。FAIMS通过滤除化学噪声提高了动态范围和离子的检测限。FAIMS也可以用来去除干扰离子物种，并选择最佳的肽电荷状态识别串联MS。在这里，我们回顾了最近的发展，LC-FAIMS-MS及其应用MS为基础的蛋白质组学。
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 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, we review recent developments in LC-FAIMS-MS and its application to MS-based proteomics.