Hydrogen-deuterium exchange of -carbon protons and fragmentation pathways in N-methylated glycine and alanine-containing peptides derivatized by quaternary ammonium salts
Hydrogen-deuterium exchange of -carbon protons and fragmentation pathways in N-methylated glycine and alanine-containing peptides derivatized by quaternary ammonium salts
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DOI：
10.1002/jms.3371
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发表时间：
2014-06-01
影响因子：
2.3
通讯作者：
Szewczuk, Zbigniew
中科院分区：
文献类型：
--
作者：
Bachor, Remigiusz;Rudowska, Magdalena;Szewczuk, Zbigniew
最近，我们开发了一种选择性和高效的方法，在模型肽的肌氨酸残基（n-甲基甘氨酸）的-碳(c)上进行氢-氘交换（HDX） [Bchor等]。[j].质谱学报，2014,49(3)。在这里，我们报道了季铵（QA）基团对肽中肌氨酸和n -甲基丙氨酸-C上HDX的影响。所得结果表明，由于QA的存在，肌肉残渣中HDX的显著加速。效果取决于肌氨酸残基与QA片段之间的距离。在-C处引入的氘核在酸性水溶液中可以抵抗反交换。在碰撞诱导解离的过程中，没有可移动氢的低聚糖肽的氘标记类似物显示了位于肌氨酸残基c位的氢的动员。版权所有：John Wiley & Sons， Ltd。
Recently, we developed a selective and efficient method of hydrogen-deuterium exchange (HDX) at the -carbon (-C) of sarcosine residue (N-methylglycine) in model peptides [Bchor et al. J. Mass Spectrom. 2014, 49, 43]. Here, we report the influence of quaternary ammonium (QA) group on HDX at the -C of sarcosine and N-methylalanine in peptides. The obtained results suggest a significant acceleration of the HDX in sarcosine residue caused by the presence of QA. The effect depends on the distance between the sarcosine residue and QA moiety. The deuterons, introduced at -C, are resistant to the back-exchange in acidic aqueous solution. The collision induced dissociation of the deuterium-labeled analogs of QA-tagged oligosarcosine peptides without mobile hydrogen revealed the mobilization of the hydrogens localized at -C of sarcosine residue. Copyright (c) 2014 John Wiley & Sons, Ltd.