Interactions of α- and β-avoparcin with bacterial cell-wall receptor-mimicking peptides studied by electrospray ionization mass spectrometry

Solution phase affinity constants of the glycopeptide antibiotic alpha- and beta-avoparcin, with a range of bacterial cell-wall receptor-mimicking model peptides, were determined by a relatively new method: affinity electrospray ionization mass spectrometry (ESI-MS). This method is relatively effici...

Full description

Saved in:
Bibliographic Details
Published in:Journal of antimicrobial chemotherapy 1999-11, Vol.44 (5), p.593-599
Main Authors: DE KERK-VAN HOOF, A. V, HECK, A. J. R
Format: Article
Language:English
Subjects:
a-Avoparcin
Anti-Bacterial Agents - chemistry
Anti-Bacterial Agents - metabolism
Antibacterial agents
Antibiotics. Antiinfectious agents. Antiparasitic agents
b-Avoparcin
Bacteria - chemistry
Bacteria - metabolism
Binding Sites
Binding, Competitive
Biological and medical sciences
Cell Wall - chemistry
Glycopeptides
Ligands
Mass Spectrometry - methods
Medical sciences
Oligopeptides - metabolism
Pharmacology. Drug treatments
solution phase affinity constants
Vancomycin - chemistry
Vancomycin - metabolism
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Solution phase affinity constants of the glycopeptide antibiotic alpha- and beta-avoparcin, with a range of bacterial cell-wall receptor-mimicking model peptides, were determined by a relatively new method: affinity electrospray ionization mass spectrometry (ESI-MS). This method is relatively efficient and allows the parallel determination of several affinity constants in mixtures of antibiotics and receptors. The determined binding constants for alpha- and beta-avoparcin were compared with those of the related glycopeptide antibiotic vancomycin. The solution phase binding affinities of alpha- and beta-avoparcin on one hand, and vancomycin on the other, were found to be in the same order, at least for the range of receptor-mimicking peptides studied. However, beta-avoparcin displayed slightly higher binding affinities than alpha-avoparcin, particularly for strong binding receptor-mimicking peptides. The evidence that alpha- and beta-avoparcin and vancomycin are structurally similar, combined with the present data revealing their similar affinity for bacterial cell-wall receptor-mimicking peptides, supports the hypothesis that the appearance of vancomycin-resistant enterococci (VRE) might be linked to the widespread use of avoparcin.
ISSN:0305-7453
1460-2091
DOI:10.1093/jac/44.5.593