Deviation from the mobile proton model in amino-modified peptides: implications for multiple reaction monitoring analysis of peptides
Deviation from the mobile proton model in amino-modified peptides: implications for multiple reaction monitoring analysis of peptides
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DOI：
10.1002/rcm.2512
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发表时间：
2006-01-01
影响因子：
2
通讯作者：
Pinto, Devanand M.
中科院分区：
文献类型：
--
作者：
Locke, Steven J.;Leslie, Andrew D.;Pinto, Devanand M.
肽断裂的研究对于理解气相中发生的化学过程以及蛋白质组分析中肽鉴定的更实际关注非常重要。使用移动质子模型作为框架，我们探讨了氨基修饰对肽碎片的影响。三个醛用于将肽的伯氨基转化为二甲氨基或杂环结构（五元或六元）。观察到的断裂模式与类似的未衍生化肽观察到的断裂模式有很大偏差。特别地，α离子是衍生肽的大多数串联质谱中的基峰。 a离子强度很大程度上取决于N端氨基酸，其中酪氨酸和苯丙氨酸的增强最强。尽管衍生肽的碎片模式发生了变化，但它们仍然提供高质量的串联质谱，在许多情况下，比未衍生肽的光谱更适合数据库搜索。此外，α, 离子的可靠存在有助于使用多反应监测方法进行快速定量测量。版权所有 (c) 2006 John Wiley & Sons, Ltd.
The study of peptide fragmentation is important to the understanding of chemical processes occurring in the gas phase and the more practical concern of peptide identification for proteomic analysis. Using the mobile proton model as a framework, we explore the effect of amino-group modifications on peptide fragmentation. Three aldehydes are used to transform the peptides' primary amino groups into either a dimethylamino or a heterocyclic structure (five- or six-membered). The observed fragmentation patterns deviate strongly from those observed for the analogous underivatised peptides. In particular, the a, ion is the base peak in most tandem mass spectra of the derivatised peptides. The a, ion intensity depends Strongly on the N-terminal amino acid, with tyrosine and phenylalanine having the strongest enhancement. Despite the change in fragmentation patterns of the derivatised peptides, they still provide high-quality tandem mass spectra that, in many cases, are more amenable to database searching than the spectra of underivatised peptides. In addition, the reliable presence of the a, ion facilitates rapid quantitative measurements using the multiple reaction monitoring approach. Copyright (c) 2006 John Wiley & Sons, Ltd.