期刊
CHEMICAL COMMUNICATIONS
卷 55, 期 19, 页码 2841-2844出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/c9cc00159j
关键词
-
资金
- Robert A. Welch Foundation [C-1680]
- National Science Foundation [CHE-1055569]
S-Arylation of cysteine residues is an increasingly powerful tool for site-specific modification of proteins, providing novel structure and electronic perturbation. The present work demonstrates an operationally-simple cysteine arylation reaction 2-nitro-substituted arylboronic acids, promoted by a simple nickel(ii) salt. The process exhibits strikingly fast reaction rates under physiological conditions in purely aqueous media with excellent selectivity toward cysteine residues. Cysteine arylation of natural proteins and peptides allows attachment of useful reactive handles for stapling, imaging, or further conjugation.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据