Batchelor, M, Zhou, DJ, Cooper, MA et al. (2 more authors) (2010) Vancomycin dimer formation between analogues of bacterial peptidoglycan surfaces probed by force spectroscopy. Organic and Biomolecular Chemistry, 8 (5). 1142 - 1148 . ISSN 1477-0520
Abstract
Functionalised thiols presenting peptides found in the peptidoglycan from 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 investigate 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.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Keywords: | vancomycin, dimerisation, atomic force microscopy, force spectroscopy, antibiotics |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Engineering & Physical Sciences (Leeds) > School of Chemistry (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 18 Jun 2013 11:31 |
Last Modified: | 04 Nov 2016 03:08 |
Published Version: | http://http//dx.doi.org%20/10.1039/b919347b |
Status: | Published |
Publisher: | Royal Society of Chemistry |
Identification Number: | 10.1039/b919347b |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:75721 |