Efficiently demonstrates broad substrate compatibility in thioglycosylation of tryptophan-containing peptides, indicating versatility in peptide synthesis.
An efficient copper-catalyzed thioglycosylation of tryptophan and tryptophan-containing peptides with N-(thioglycosyl)succinimide has been developed. The methodology demonstrates broad substrate compatibility, encompassing diverse glycan donors (hexoses, pentoses, and disaccharides) and peptide backbones (di-, tri-, and tetrapeptides). Furthermore, the protocol was extended to S-arylation, S-alkylation, cysteinylation, thiocyanation, and selenoarylation, showcasing its versatility.
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Wei et al. (2026) studied this question.
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