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首页> 外文期刊>Journal of the American Society for Mass Spectrometry >Enhanced Characterization of Singly Protonated Phosphopeptide Ions by Femtosecond Laser-induced Ionization/Dissociation Tandem Mass Spectrometry (fs-LID-MS/MS)
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Enhanced Characterization of Singly Protonated Phosphopeptide Ions by Femtosecond Laser-induced Ionization/Dissociation Tandem Mass Spectrometry (fs-LID-MS/MS)

机译：飞秒激光诱导的电离/解离串联质谱（fs-LID-MS / MS）增强了对单质子化磷酸肽离子的表征

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摘要

To develop an improved understanding of the regulatory role that post-translational modifications (PTMs) involving phosphorylation play in the maintenance of normal cellular function, tandem mass spectrometry (MS/MS) strategies coupled with ion activation techniques such as collision-induced dissociation (CID) and electron-transfer dissociation (ETD) are typically employed to identify the presence and site-specific locations of the phosphate moieties within a given phosphoprotein of interest. However, the ability of these techniques to obtain sufficient structural information for unambiguous phosphopeptide identification and characterization is highly dependent on the ion activation method employed and the properties of the precursor ion that is subjected to dissociation. Herein, we describe the application of a recently developed alternative ion activation technique for phosphopeptide analysis, termed femtosecond laser-induced ionization/dissociation (fs-LID). In contrast to CID and ETD, fs-LID is shown to be particularly suited to the analysis of singly protonated phosphopeptide ions, yielding a wide range of product ions including a, b, c, x, y, and z sequence ions, as well as ions that are potentially diagnostic of the positions of phosphorylation (e.g., 'a_n+1-98'). Importantly, the lack of phosphate moiety losses or phosphate group 'scrambling' provides unambiguous information for sequence identification and phosphorylation site characterization. Therefore, fs-LID-MS/MS can serve as a complementary technique to established methodologies for phosphoproteomic analysis.
机译：为了更好地理解涉及磷酸化的翻译后修饰（PTM）在维持正常细胞功能中的调控作用，串联质谱分析（MS / MS）策略结合离子激活技术（例如碰撞诱导解离（CID）） ）和电子转移解离（ETD）通常用于鉴定给定目标磷蛋白中磷酸部分的存在和位点特异性位置。但是，这些技术获得足够的结构信息以进行明确的磷酸肽鉴定和表征的能力高度依赖于所采用的离子活化方法和经历离解的前体离子的性质。在这里，我们描述了一种最新开发的替代离子激活技术在磷酸肽分析中的应用，称为飞秒激光诱导的电离/解离（fs-LID）。与CID和ETD相比，fs-LID被证明特别适用于分析单质子化的磷酸肽离子，产生的产物离子范围也很广，包括a，b，c，x，y和z序列离子。作为可能诊断磷酸化位置的离子（例如“ a_n + 1-98”）。重要的是，缺少磷酸部分的丢失或磷酸基团“加扰”为序列鉴定和磷酸化位点表征提供了明确的信息。因此，fs-LID-MS / MS可以作为已建立的磷酸蛋白质组学分析方法的补充技术。

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