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Issue 17, 2018
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A route to diastereomerically pure phenylglycine thioester peptides: crucial intermediates for investigating glycopeptide antibiotic biosynthesis

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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.

Graphical abstract: A route to diastereomerically pure phenylglycine thioester peptides: crucial intermediates for investigating glycopeptide antibiotic biosynthesis

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Publication details

The article was received on 08 Dec 2017, accepted on 29 Jan 2018 and first published on 09 Feb 2018


Article type: Communication
DOI: 10.1039/C7CC09409D
Citation: Chem. Commun., 2018,54, 2146-2149
  • Open access: Creative Commons BY license
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    A route to diastereomerically pure phenylglycine thioester peptides: crucial intermediates for investigating glycopeptide antibiotic biosynthesis

    J. Tailhades, M. Schoppet, A. Greule, M. Peschke, C. Brieke and M. J. Cryle, Chem. Commun., 2018, 54, 2146
    DOI: 10.1039/C7CC09409D

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