Tryptophan-specific peptide modification through metal-free photoinduced N-H alkylation employing N-aryl glycines
作者机构:School of Medicine or Institute of Translation MedicineShanghai UniversityShanghai 200444China
出 版 物:《Chinese Chemical Letters》 (中国化学快报(英文版))
年 卷 期:2024年第35卷第6期
页 面:316-319页
核心收录:
学科分类:081704[工学-应用化学] 07[理学] 08[工学] 0817[工学-化学工程与技术] 070303[理学-有机化学] 0703[理学-化学]
基 金:the financial support from the National Natural Science Foundation of China(No.22107062) the National Natural Science Foundation of Shanghai(No.21ZR1422600)
主 题:Tryptophan Peptide Modification Glycine Photoinduced
摘 要:Tryptophan(Trp)carries a unique heteroaromatic indole side chain and plays a critical role in peptide or protein ***,we have reported a metal-free photoinduced N-H alkylation strategy using N-aryl glycines for specific modification of tryptophan-containing *** robustness of our approach is demonstrated by its wide substrate scope,excellent isolated yields,as well as almost unobservable side *** this highly efficiently metal-free condition,alkylated Trp-containing peptides can be smoothly *** study provides a reliable and practical tool for the chemo-selective modification of various tryptophan containing oligopeptides.