A route to diastereomerically pure phenylglycine thioester peptides

Crucial intermediates for investigating glycopeptide antibiotic biosynthesis

Julien Tailhades, Melanie Schoppet, Anja Greule, Madeleine Peschke, Clara Brieke, Max J. Cryle

Research output: Contribution to journalArticleResearchpeer-review

Abstract

Non-ribosomal peptides contain an array of amino acid building blocks that can present challenges for the synthesis of important intermediates. Here, we report the synthesis of glycopeptide antibiotic (GPA) thioester peptides that retains the crucial stereochemical purity of the terminal phenylglycine residue, which we show is essential for the enzymatic GPA cyclisation cascade.

Original languageEnglish
Pages (from-to)2146-2149
Number of pages4
JournalChemical Communications
Volume54
Issue number17
DOIs
Publication statusPublished - 9 Feb 2018

Cite this

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A route to diastereomerically pure phenylglycine thioester peptides : Crucial intermediates for investigating glycopeptide antibiotic biosynthesis. / Tailhades, Julien; Schoppet, Melanie; Greule, Anja; Peschke, Madeleine; Brieke, Clara; Cryle, Max J.

In: Chemical Communications, Vol. 54, No. 17, 09.02.2018, p. 2146-2149.

Research output: Contribution to journalArticleResearchpeer-review

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AU - Cryle, Max J.

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