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

Cheng, Mu, Ziora, Zyta M., Hansford, Karl A., Blaskovich, Mark A., Butler, Mark S. and Cooper, Matthew A. (2014) Anti-cooperative ligand binding and dimerisation in the glycopeptide antibiotic dalbavancin. Organic and Biomolecular Chemistry, 12 16: 2568-2575. doi:10.1039/c3ob42428f

Author Cheng, Mu
Ziora, Zyta M.
Hansford, Karl A.
Blaskovich, Mark A.
Butler, Mark S.
Cooper, Matthew A.
Title Anti-cooperative ligand binding and dimerisation in the glycopeptide antibiotic dalbavancin
Journal name Organic and Biomolecular Chemistry   Check publisher's open access policy
ISSN 1477-0520
Publication date 2014-04-28
Year available 2014
Sub-type Article (original research)
DOI 10.1039/c3ob42428f
Open Access Status DOI
Volume 12
Issue 16
Start page 2568
End page 2575
Total pages 8
Place of publication Cambridge, United Kingdom
Publisher Royal Society of Chemistry
Language eng
Subject 1606 Political Science
1605 Policy and Administration
1303 Specialist Studies in Education
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. This journal is
Keyword Chemistry, Organic
Q-Index Code C1
Q-Index Status Confirmed Code
Grant ID 094977
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2015 Collection
Institute for Molecular Bioscience - Publications
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Created: Thu, 10 Apr 2014, 20:58:01 EST by Susan Allen on behalf of Institute for Molecular Bioscience