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

20 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

UN SDGs

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

SDG 3 Good Health and Well-being

ASJC Scopus subject areas

Biochemistry
Physical and Theoretical Chemistry
Organic Chemistry

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10.1021/ol2017356

Cite this

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title = "Peptide ligations accelerated by N-terminal aspartate and glutamate residues",

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.

UR - https://www.scopus.com/pages/publications/80052771002

UR - https://www.scopus.com/pages/publications/80052771002#tab=citedBy

U2 - 10.1021/ol2017356

DO - 10.1021/ol2017356

M3 - Article

C2 - 21830797

AN - SCOPUS:80052771002

SN - 1523-7060

VL - 13

SP - 4770

EP - 4773

JO - Organic Letters

JF - Organic Letters

IS - 18

ER -

Peptide ligations accelerated by N-terminal aspartate and glutamate residues

Abstract

UN SDGs

ASJC Scopus subject areas

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