Allenamides as Orthogonal Handles for Selective Modification of Cysteine in Peptides and Proteins
Allenamides as Orthogonal Handles for Selective Modification of Cysteine in Peptides and Proteins
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DOI：
10.1002/anie.201403121
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发表时间：
2014-07-14
影响因子：
16.6
通讯作者：
Loh, Teck-Peng
中科院分区：
文献类型：
--
作者：
Abbas, Ata;Xing, Bengang;Loh, Teck-Peng
在这项研究中，已经成功地开发了一种非常简单和直接的策略来选择性地标记完全不受保护的多肽和蛋白质中的目标半胱氨酸残基。该策略基于烯丙酰胺与半胱氨酸硫醇的反应，在水介质中快速进行，具有良好的选择性和定量转化率，从而形成稳定的不可逆偶联物。该工艺的简单性和温和性相结合，使联苯二胺成为以半胱氨酸为靶标的坚固和通用的手柄，并在生物系统中具有潜在的用途。此外，荧光标记研究表明，在各种感兴趣的分子上安装C端烯丙酰胺部分可能为含半胱氨酸的蛋白质的位点特异性标记提供一种新的方法。因此，这种新的标记策略可能会为其在生命科学领域的应用打开一扇窗。
In this study, a remarkably simple and direct strategy has been successfully developed to selectively label target cysteine residues in fully unprotected peptides and proteins. The strategy is based on the reaction between allenamides and the cysteine thiol, and proceeds swiftly in aqueous medium with excellent selectivity and quantitative conversion, thus forming a stable and irreversible conjugate. The combined simplicity and mildness of the process project allenamide as robust and versatile handles to target cysteines and has potential use in biological systems. Additionally, fluorescent-labeling studies demonstrated that the installation of a C-terminal allenamide moiety onto various molecules of interest may supply a new methodology towards the site-specific labeling of cysteine-containing proteins. Such a new labeling strategy may thus open a window for its application in the field of life sciences.