Peptide ligations accelerated by N-terminal aspartate and glutamate residues

Gemma L. Thomas; Yves S.Y. Hsieh; Candy K.Y. Chun; Zheng Li Cai; Jeffrey R. Reimers; Richard J. Payne

doi:10.1021/ol2017356

Peptide ligations accelerated by N-terminal aspartate and glutamate residues

Gemma L. Thomas, Yves S.Y. Hsieh, Candy K.Y. Chun, Zheng Li Cai, Jeffrey R. Reimers, Richard J. Payne

Research output: Contribution to journal › Article › peer-review

18 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	4770-4773
Number of pages	4
Journal	Organic Letters
Volume	13
Issue number	18
DOIs	https://doi.org/10.1021/ol2017356
Publication status	Published - Sept 16 2011
Externally published	Yes

ASJC Scopus subject areas

Biochemistry
Physical and Theoretical Chemistry
Organic Chemistry

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1021/ol2017356

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abstract = "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.",

author = "Thomas, {Gemma L.} and Hsieh, {Yves S.Y.} and Chun, {Candy K.Y.} and Cai, {Zheng Li} and Reimers, {Jeffrey R.} and Payne, {Richard J.}",

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AU - Thomas, Gemma L.

AU - Hsieh, Yves S.Y.

AU - Chun, Candy K.Y.

AU - Cai, Zheng Li

AU - Reimers, Jeffrey R.

AU - Payne, Richard J.

PY - 2011/9/16

Y1 - 2011/9/16

N2 - 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.

AB - 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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Peptide ligations accelerated by N-terminal aspartate and glutamate residues

Abstract

ASJC Scopus subject areas

UN SDGs

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