Late-stage C(sp ²)–H and C(sp ³)–H glycosylation of C-aryl/alkyl glycopeptides: mechanistic insights and fluorescence labeling†‡

Abstract

C(sp ³)–H and C(sp ²)–H glycosylations of structurally complex amino acids and peptides were accomplished through the assistance of triazole peptide-isosteres. The palladium-catalyzed peptide–saccharide conjugation provided modular access to structurally complex C-alkyl glycoamino acids, glycopeptides and C-aryl glycosides, while enabling the assembly of fluorescent-labeled glycoamino acids. The C–H activation approach represents an expedient and efficient strategy for peptide late-stage diversification in a programmable as well as chemo-, regio-, and diastereo-selective fashion.

Abstract

C–H glycosylations of complex amino acids and peptides were accomplished through the assistance of triazole peptide-isosteres. The palladium-catalyzed glycosylation provided access to complex C-glycosides and fluorescent-labeled glycoamino acids.