Macrocyclization of bioactive peptides with internal thiazole motifs <i>via</i> palladium-catalyzed C–H olefination
Chuangxu Cai, Feifei Wang, Xiuyun Xiao, Wangjian Sheng, Shu Liu, Jun Chen, Jie Zheng, Ran Xie, Zengbing Bai, Huan Wang
Abstract
)-H olefination. In this protocol, the thiazole and neighboring amide bonds act as directing groups, which allows site-specific olefination of phenylalanine, tryptophan and tyrosine residues. This chemistry exhibits broad substrate scope and provides facile access to peptide-peptide conjugates and peptide macrocycles. Our results highlight the potency and applicability of thiazole motifs in promoting Pd-catalyzed functionalization of peptides.
Topics & Concepts
ThiazoleChemistryCombinatorial chemistryPeptidePalladiumStereochemistryTyrosineAmideCatalysisPhenylalanineTryptophanAmino acidOrganic chemistryBiochemistryCatalytic C–H Functionalization MethodsChemical Synthesis and AnalysisClick Chemistry and Applications