Reversibly switching the conformation of short peptide through in-tether chiral sulfonium auxiliary  

作　　者：Xiaodong Shi Yixiang Jiang Dan Yang Hui Zhao Yuan Tian Zigang Li 

机构地区：[1]School of Chemical Biology and Biotechnology, Peking University Shenzhen Graduate School [2]School of Life Science and Engineering, Southwest Jiaotong University

出　　处：《Chinese Chemical Letters》2018年第3期485-488,共4页中国化学快报（英文版）

基　　金：financial support from the National Natural Science Foundation of China(Nos. 21372023 and 81572198);Ministry of Science and Technology of the People's Republic of China(No. 2015DFA31590);the Shenzhen Science and Technology Innovation Committee(Nos. JSGG20140519105550503, JCYJ20150331100849958,JCYJ20150403101146313, JCYJ20160301111338144,JCYJ20160331115853521, JSGG20160301095829250 and ZDSYS201504301539161);the Shenzhen Peacock Program(No. KQTD201103)

摘　　要：A chirality induced helicity method has been developed to modulate the peptide＇s biophysical and biochemical properties. We report herein a novel approach for reversibly switching the conformation of short constraint a-helical peptides through alkylation of the in-tether thioether and dealkylation of the chiral sulfonium. This traceless redox sensitive tagging strategy broadened our scope of CIH （chirality induced helicity） strategy and provided a valuable approach to functionalize the peptide tether.A chirality induced helicity method has been developed to modulate the peptide＇s biophysical and biochemical properties. We report herein a novel approach for reversibly switching the conformation of short constraint a-helical peptides through alkylation of the in-tether thioether and dealkylation of the chiral sulfonium. This traceless redox sensitive tagging strategy broadened our scope of CIH （chirality induced helicity） strategy and provided a valuable approach to functionalize the peptide tether.

关 键 词：Cyclic peptide Sulfonium Chiral center α-Helix Reversible Tether modification 

分 类 号：O629.72[理学—有机化学]