Glycopeptide ligation via direct aminolysis of selenoester

Autor:	Wen-Bo Xu, Chang-Wei Wang, Jing-Jing Du, Ze Lei, Lian Zhang, Jun Guo, Xiao-Fei Gao, Shi-Yao Zou, Ling-Ming Xin
Rok vydání:	2018
Předmět:	chemistry.chemical_classification 010405 organic chemistry Peptide General Chemistry 010402 general chemistry 01 natural sciences Combinatorial chemistry Glycopeptide 0104 chemical sciences Amino acid Residue (chemistry) chemistry.chemical_compound Aminolysis chemistry Amide Epimer Cysteine
Zdroj:	Chinese Chemical Letters. 29:1127-1130
ISSN:	1001-8417
DOI:	10.1016/j.cclet.2018.04.016
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::d7c0541f43ae63682851d68189871bed https://doi.org/10.1016/j.cclet.2018.04.016 Zobrazit plný text záznamu Full Text from ScienceDirect