Chemical Syntheses and Biological Evaluation of CXCL14 and Its Site-Selectively Modified Methionine Sulfoxide-Containing Derivatives

Chemical Syntheses and Biological Evaluation of CXCL14 and Its Site-Selectively Modified Methionine Sulfoxide-Containing Derivatives
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CXCL14及其位点选择性修饰的蛋氨酸亚砜衍生物的化学合成和生物学评价

DOI:
10.1021/acs.joc.9b02730
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发表时间:
2020-02-07
影响因子:
3.6
通讯作者:
Dong, Suwei
Dong, Suwei
中科院分区:
化学2区
文献类型:
--
作者:
Cai, Zonghui;Wei, Qijia;Dong, Suwei

文献摘要

被引文献

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对于研究这种重要的翻译后修饰(PTM),获得含有蛋氨酸亚砜[Met(O)]的蛋白质特别有价值。然而,由于缺乏选择性的体外氧化方法,很难获得准确、可控地掺入Met(O)的均一蛋白质,特别是含有多种蛋氨酸的蛋白质。在这里,我们报道了一种化学方法来选择性地合成蛋氨酸氧化的人趋化因子CXCL14。并对合成蛋白的体外趋化活性进行了评价。
The access to methionine sulfoxide [Met(O)]-containing proteins is particularly valuable for studying this important type of post-translational modification (PTM). However, the lack of selective in vitro oxidation methods makes it difficult to obtain homogeneous proteins with accurate and controllable incorporation of Met(O), particularly the ones with multiple methionines. Here, we report a chemical approach to synthesize methionine-oxidized human chemokine CXCL14 in a site-selective manner. The in vitro chemotaxis activities of synthetic proteins have also been evaluated.