Vancomycin dimer formation between analogues of bacterial peptidoglycan surfaces probed by force spectroscopy.
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.
Batchelor
Matthew
M
Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, UK CB2 1EW. m.r.batchelor.98@cantab.net
Zhou
Dejian
D
Cooper
Matthew A
MA
Abell
Chris
C
Rayment
Trevor
T
D000900:Anti-Bacterial Agents / Q000378:metabolism*; D001419:Bacteria / Q000737:chemistry / Q000378:metabolism*; D032701:Biomimetics; D002473:Cell Wall / Q000737:chemistry / Q000378:metabolism; D019281:Dimerization; D024881:Drug Resistance, Bacterial; D018625:Microscopy, Atomic Force; D010457:Peptidoglycan / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D014640:Vancomycin / Q000378:metabolism*
D000900:Anti-Bacterial Agents; D010457:Peptidoglycan; D014640:Vancomycin