Issue 5, 2010
From the journal:

Organic & Biomolecular Chemistry

Vancomycin dimer formation between analogues of bacterial peptidoglycan surfaces probed by force spectroscopy†

Matthew Batchelor,‡*a   Dejian Zhou,b   Matthew A. Cooper,c   Chris Abella  and  Trevor Raymentd  

* Corresponding authors

a Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, UK
E-mail: m.r.batchelor.98@cantab.net

b School of Chemistry and the Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, UK

c Institute for Molecular Bioscience, The University of Queensland, Brisbane, Australia

d School of Chemistry, University of Birmingham, Birmingham, UK

Abstract

Functionalised thiols presenting peptides found in the peptidoglycan of vancomycin-sensitive and -resistant bacteria were synthesised and used to form self-assembled monolayers (SAMs) on gold surfaces. This model bacterial cell-wall surface mimic was used to study binding interactions with vancomycin. Force spectroscopy, using the atomic force microscope (AFM), was used to investigate the specific rupture of interfacial vancomycin dimer complexes formed between pairs of vancomycin molecules bound to peptide-coated AFM probe and substrate surfaces. Clear adhesive contacts were observed between the vancomycin-sensitive peptide surfaces when vancomycin was present in solution, and the adhesion force demonstrated a clear dependence on antibiotic concentration.

Graphical abstract: Vancomycin dimer formation between analogues of bacterial peptidoglycan surfaces probed by force spectroscopy

About
Cited by
Related
Download options Please wait...

Supplementary files

Article information

DOI
https://doi.org/10.1039/B919347B
Article type
Paper
Submitted
17 Sep 2009
Accepted
26 Nov 2009
First published
08 Jan 2010

Org. Biomol. Chem., 2010,8, 1142-1148

Permissions

Request permissions

Vancomycin dimer formation between analogues of bacterial peptidoglycan surfaces probed by force spectroscopy

M. Batchelor, D. Zhou, M. A. Cooper, C. Abell and T. Rayment, Org. Biomol. Chem., 2010, 8, 1142 DOI: 10.1039/B919347B

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements