Molecular interactions of glycopeptide antibiotics investigated by affinity capillary electrophoresis and bioaffinity electrospray ionization-mass spectrometry.
Many analytical approaches are available to evaluate (bio)molecular interactions, all of which have their particular advantages and disadvantages. In recent years, two relatively new techniques have emerged that may be used by the bioanalytical community to evaluate such interactions, namely affinity capillary electrophoresis (ACE) and bioaffinity electrospray ionization-mass spectrometry (ESI-MS). In this paper, we describe and evaluate the use of both these techniques for the investigation of the interactions of glycopeptide antibiotics with peptides that mimic the bacterial cell wall binding site. We focus particularly on the effect of the sugar moieties attached to the antibiotic peptide backbone and on the noncovalent dimerization of these glycopeptide antibiotics.
Vollmerhaus
Pauline J
PJ
Department of Biomolecular Mass Spectrometry, Bijvoet Center for Biomolecular Research, Utrecht University, Sorbonelaan 16, NL-3584 CA Utrecht, The Netherlands.
Tempels
F W Alexander
FW
Kettenes-van den Bosch
J Jantina
JJ
Heck
Albert J R
AJ
D000900:Anti-Bacterial Agents / Q000032:analysis*; D019075:Electrophoresis, Capillary / Q000379:methods*; D006020:Glycopeptides; D006801:Humans; D021241:Spectrometry, Mass, Electrospray Ionization / Q000379:methods*
D000900:Anti-Bacterial Agents; D006020:Glycopeptides