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首页> 外文期刊>Journal of mass spectrometry: JMS >The unusual hydrogen-deuterium exchange of α-carbon protons in N-substituted glycinecontaining peptides
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The unusual hydrogen-deuterium exchange of α-carbon protons in N-substituted glycinecontaining peptides

机译：N-取代的含甘氨酸的肽中α-碳质子的异常氢-氘交换

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摘要

Hydrogens connected to α-carbon (α-C) of amino acid residues are usually resistant to hydrogen-deuterium exchange (HDX) unless reaction conditions promote racemization. Although N-methylglycine (sarcosine) residue has been found in biologically active peptide such as cyclosporine, to the best of our knowledge, the HDX of α-C protons of this residue was not explored yet. Here, we presented a new and efficient methodology of α-C deuteration in sarcosine residues under basic aqueous conditions. The deuterons, introduced at α-C atom, do not undergo back-exchange in acidic aqueous solution. The electrospray ionization- MS and MS/MS experiments on proposed model peptides confirmed the HDX at α-C and revealed the unexpected hydrogen scrambling in sarcosine-containing peptides. Although the observed HDX of α-C protons is only successful in N-acylglycine when the amide possesses a certain degree of alkylation, it offers a new approach to the analysis of sarcosine-containing peptides such as cyclosporine.
机译：除非反应条件促进外消旋作用，否则与氨基酸残基的α-碳（α-C）连接的氢通常会抵抗氢-氘交换（HDX）。尽管在生物活性肽（例如环孢菌素）中发现了N-甲基甘氨酸（肌氨酸）残基，但据我们所知，尚未探索该残基的α-C质子的HDX。在这里，我们介绍了一种在碱性水溶液条件下肌氨酸残基中α-C氘化的新方法。在α-C原子处引入的氘核在酸性水溶液中不会发生反向交换。对建议的模型肽进行的电喷雾电离-MS和MS / MS实验在α-C处证实了HDX，并揭示了含肌氨酸肽中意外的氢加扰。尽管当酰胺具有一定程度的烷基化时，观察到的α-C质子的HDX仅在N-酰基甘氨酸中成功，但它为分析含肌氨酸的肽（例如环孢霉素）提供了新的方法。

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