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 journalArticle

17 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 languageEnglish
Pages (from-to)4770-4773
Number of pages4
JournalOrganic Letters
Volume13
Issue number18
DOIs
Publication statusPublished - Sep 16 2011
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Physical and Theoretical Chemistry
  • Organic Chemistry

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  • Cite this

    Thomas, G. L., Hsieh, Y. S. Y., Chun, C. K. Y., Cai, Z. L., Reimers, J. R., & Payne, R. J. (2011). Peptide ligations accelerated by N-terminal aspartate and glutamate residues. Organic Letters, 13(18), 4770-4773. https://doi.org/10.1021/ol2017356