Peptide Ligations Accelerated by N-Terminal Aspartate and Glutamate Residues

被引：17
|
作者：
Thomas, Gemma L. [1 ]
Hsieh, Yves S. Y. [1 ]
Chun, Candy K. Y. [1 ]
Cai, Zheng-Li [1 ]
Reimers, Jeffrey R. [1 ]
Payne, Richard J. [1 ]
机构：
[1] Univ Sydney, Sch Chem, Sydney, NSW 2006, Australia
来源：
ORGANIC LETTERS | 2011年 / 13卷 / 18期
基金：
澳大利亚研究理事会;
关键词：
NATIVE CHEMICAL LIGATION; SUGAR-ASSISTED LIGATION; CYSTEINE-FREE PEPTIDE; PROTEIN-SYNTHESIS; CHEMOSELECTIVE LIGATION; GLYCOPROTEIN; THIOESTERS; STRATEGIES; MECHANISM;
D O I：
10.1021/ol2017356
中图分类号：
O62 [有机化学];
学科分类号：
070303 ; 081704 ;
摘要：
A novel application of intramolecular base catalysis confers enhanced reaction rates for aminolysis ligations between peptide thioesters and peptides bearing N-terminal aspartate or glutamate residues. The broad scope of this process and its application in the total synthesis of the diabetes drug exenatide is demonstrated.
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页码：4770 / 4773
页数：4
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