Jump to main content
Jump to site search

Issue 16, 2014
Previous Article Next Article

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

Author affiliations

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

Back to tab navigation
Please wait while Download options loads

Supplementary files

Publication details

The article was received on 05 Dec 2013, accepted on 22 Jan 2014 and first published on 10 Mar 2014


Article type: Paper
DOI: 10.1039/C3OB42428F
Citation: Org. Biomol. Chem., 2014,12, 2568-2575
  • Open access: Creative Commons BY license
  •   Request permissions

    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

    This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. Material from this article can be used in other publications provided that the correct acknowledgement is given with the reproduced material.

    Reproduced material should be attributed as follows:

    • For reproduction of material from NJC:
      [Original citation] - Published by The Royal Society of Chemistry (RSC) on behalf of the Centre National de la Recherche Scientifique (CNRS) and the RSC.
    • For reproduction of material from PCCP:
      [Original citation] - Published by the PCCP Owner Societies.
    • For reproduction of material from PPS:
      [Original citation] - Published by The Royal Society of Chemistry (RSC) on behalf of the European Society for Photobiology, the European Photochemistry Association, and RSC.
    • For reproduction of material from all other RSC journals:
      [Original citation] - Published by The Royal Society of Chemistry.

    Information about reproducing material from RSC articles with different licences is available on our Permission Requests page.

Search articles by author