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 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.展开更多
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)+1 种基金the Shenzhen Science and Technology Innovation Committee(Nos. JSGG20140519105550503, JCYJ20150331100849958,JCYJ20150403101146313, JCYJ20160301111338144,JCYJ20160331115853521, JSGG20160301095829250 and ZDSYS201504301539161)the Shenzhen Peacock Program(No. KQTD201103)
文摘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.
