Issue 17, 2018

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

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

Supplementary files

Article information

Article type
Communication
Submitted
08 Dec 2017
Accepted
29 Jan 2018
First published
09 Feb 2018
This article is Open Access
Creative Commons BY license

Chem. Commun., 2018,54, 2146-2149

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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