Yuena Wang, Rongtong Zhao, Chuan Wan, Xiaochun Guo, Fenfang Yang, Zhanfeng Hou, Rui Wang, Shuiming Li, Tiejian Feng, Feng Yin, and Zigang Li
Organic Letters 2022 24 (39), 7205-7209
DOI: 10.1021/acs.orglett.2c02974
The ligand-directed (LD) chemistry provides powerful tools for site-specific modification of proteins. We utilized a peptide with an appended methionine (Met) as a ligand; then, the Met thioether was modified into sulfonium which enabled a proximity induced group transfer onto protein cysteine in the vicinity upon peptide–target binding. The sulfonium warhead could be easily constructed with unprotected peptides, and the transferable group scope was conducted on model protein PDZ and its ligand peptides. In addition, a living cell labeling was successfully achieved.
