Centre for Analytical Science, Department of Chemistry, Loughborough University, Loughborough, Leicestershire, LE11 3TU, United Kingdom.
Anal Chem. 2010 Dec 1;82(23):9827-34. doi: 10.1021/ac102125u. Epub 2010 Nov 4.
Miniaturized ultra high field asymmetric waveform ion mobility spectrometry (ultra-FAIMS) combined with mass spectrometry (MS) has been applied to the analysis of standard and tryptic peptides, derived from α-1-acid glycoprotein, using electrospray and nanoelectrospray ion sources. Singly and multiply charged peptide ions were separated in the gas phase using ultra-FAIMS and detected by ion trap and time-of-flight MS. The small compensation voltage (CV) window for the transmission of singly charged ions demonstrates the ability of ultra-FAIMS-MS to generate pseudo-peptide mass fingerprints that may be used to simplify spectra and identify proteins by database searching. Multiply charged ions required a higher CV for transmission, and ions with different amino acid sequences may be separated on the basis of their differential ion mobility. A partial separation of conformers was also observed for the doubly charged ion of bradykinin. Selection on the basis of charge state and differential mobility prior to tandem mass spectrometry facilitates peptide and protein identification by allowing precursor ions to be identified with greater selectivity, thus reducing spectral complexity and enhancing MS detection.
采用电喷雾和纳喷雾离子源，将微型超高效场非对称波形离子迁移谱（ultra-FAIMS）与质谱（MS）联用，对来源于α-1-酸性糖蛋白的标准肽和胰酶肽进行了分析。使用 ultra-FAIMS 在气相中分离单电荷和多电荷肽离子，并通过离子阱和飞行时间 MS 进行检测。单电荷离子的小补偿电压（CV）窗口表明 ultra-FAIMS-MS 能够生成伪肽质量指纹图谱，可用于简化图谱并通过数据库搜索鉴定蛋白质。多电荷离子的传输需要更高的 CV，并且具有不同氨基酸序列的离子可能基于它们的差分离子迁移而分离。缓激肽的二价离子也观察到部分构象分离。在串联质谱之前基于电荷状态和差分迁移率进行选择，通过提高前体离子的选择性来实现肽和蛋白质的鉴定，从而降低谱图复杂性并增强 MS 检测。
