重新审视硒代甲硫氨酸处的连接：对硒代半胱氨酸和高硒代半胱氨酸处的天然化学连接的见解。
Revisiting ligation at selenomethionine: Insights into native chemical ligation at selenocysteine and homoselenocysteine.
作者信息
Dardashti Rebecca Notis, Metanis Norman
机构信息
Institute of Chemistry, The Hebrew University of Jerusalem, Safra Campus Givat Ram, Jerusalem 91904, Israel.
Institute of Chemistry, The Hebrew University of Jerusalem, Safra Campus Givat Ram, Jerusalem 91904, Israel.
出版信息
Bioorg Med Chem. 2017 Sep 15;25(18):4983-4989. doi: 10.1016/j.bmc.2017.05.006. Epub 2017 May 5.
Selenomethionine (Sem) has been incorporated recombinantly into proteins many times to elucidate their structure and function. In this paper, we revisit incorporation via chemical protein synthesis to shed light on the mechanism of native chemical ligation. The effect of chalcogen position on ligation is investigated, and selenium-containing peptide ligation is optimized. Additionally, selective methylation is performed on selenolates in a peptide in the presence of unprotected thiols.
硒代蛋氨酸（Sem）已多次通过重组方式掺入蛋白质中，以阐明其结构和功能。在本文中，我们通过化学蛋白质合成重新审视其掺入过程，以深入了解天然化学连接的机制。研究了硫属元素位置对连接的影响，并优化了含硒肽的连接。此外，在存在未保护硫醇的情况下，对肽中的硒醇盐进行了选择性甲基化。
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