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Issue 16, 2014
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Anti-cooperative ligand binding and dimerisation in the glycopeptide antibiotic dalbavancin

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Abstract

Dalbavancin, a semi-synthetic glycopeptide with enhanced antibiotic activity compared to vancomycin and teicoplanin, binds to the C-terminal lysyl-D-alanyl-D-alanine subunit of Lipid II, inhibiting peptidoglycan biosynthesis. In this study, micro-calorimetry and electrospray ionization (ESI)-MS have been used to investigate the relationship between oligomerisation of dalbavancin and binding of a Lipid II peptide mimic, diacetyl-Lys-D-Ala-D-Ala (Ac2-Kaa). Dalbavancin dimerised strongly in an anti-cooperative manner with ligand-binding, as was the case for ristocetin A, but not for vancomycin and teicoplanin. Dalbavancin and ristocetin A both adopt an ‘closed’ conformation upon ligand binding, suggesting anti-cooperative dimerisation with ligand-binding may be a general feature of dalbavancin/ristocetin A-like glycopeptides. Understanding these effects may provide insight into design of novel dalbavancin derivatives with cooperative ligand-binding and dimerisation characteristics that could enhance antibiotic activity.

Graphical abstract: Anti-cooperative ligand binding and dimerisation in the glycopeptide antibiotic dalbavancin

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Supplementary files

Article information


Submitted
05 Dec 2013
Accepted
22 Jan 2014
First published
10 Mar 2014

This article is Open Access

Org. Biomol. Chem., 2014,12, 2568-2575
Article type
Paper
Author version available

Anti-cooperative ligand binding and dimerisation in the glycopeptide antibiotic dalbavancin

M. Cheng, Z. M. Ziora, K. A. Hansford, M. A. Blaskovich, M. S. Butler and M. A. Cooper, Org. Biomol. Chem., 2014, 12, 2568
DOI: 10.1039/C3OB42428F

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