Direct aminolysis of selenoester in aqueous media was investigated as a glycopeptide ligation strategy.This strategy allows the peptide and glycopeptide ligation to proceed smoothly(even with hindered amino acids) wit...Direct aminolysis of selenoester in aqueous media was investigated as a glycopeptide ligation strategy.This strategy allows the peptide and glycopeptide ligation to proceed smoothly(even with hindered amino acids) without the need of cysteine residue, N-terminal thiol auxiliary or coupling additive, and to afford the corresponding amide products in excellent yields. No epimerization was observed during ligation reations. In this work, the selenoester of unprotected glycopeptide was readily prepared, and the direct aminolysis of glycopeptide selenoester was successfully applied to synthesize MUC1 mucin sequence efficiently.展开更多
基金supported by the National Key Research and Development Program of China (No. 2017YFA0505200)the National Natural Science Foundation of China (No. 21772056)+2 种基金Jiangxi Key Laboratory for Mass Spectrometry and Instrumentation Open Foundation (No. JXMS201701)the self-determined research funds of CCNU from the colleges' basic research and operation of MOE (No. CCNU18TS011)the Program of Introducing Talents of Discipline to Universities of China(111 program, No. B17019)
文摘Direct aminolysis of selenoester in aqueous media was investigated as a glycopeptide ligation strategy.This strategy allows the peptide and glycopeptide ligation to proceed smoothly(even with hindered amino acids) without the need of cysteine residue, N-terminal thiol auxiliary or coupling additive, and to afford the corresponding amide products in excellent yields. No epimerization was observed during ligation reations. In this work, the selenoester of unprotected glycopeptide was readily prepared, and the direct aminolysis of glycopeptide selenoester was successfully applied to synthesize MUC1 mucin sequence efficiently.
