Molecular interactions of glycopeptide antibiotics investigated by affinity capillary electrophoresis and bioaffinity electrospray ionization‐mass spectrometry

Abstract

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.

Probing factors affecting the gas phase stabilities of noncovalent complexes formed by peptides bound to the Grb2 SH2 domain protein

“…5 titration curves were constructed by determining the ratio of peak areas of the protein-peptide complex divided by the sum of the peak areas of both the complex and the free protein similarly as described previously. 39,41,42 Experiments were performed twice giving similar results and the average values taken for analysis. It is worth mentioning that our ESI MS results aimed only at a semi-quantitative interpretation.…”

Experimental and Theoretical Studies of the Structures and Interactions of Vancomycin Antibiotics with Cell Wall Analogues

“…It is known that vancomycin prevents the growth of the bacterial cell wall by binding to the cell-wall peptidoglycan precursors terminating in -L-Lys-D-Ala-D-Ala. [1][2][3][4] Molecular recognition between vancomycin and -D-Ala-D-Ala containing peptide ligands has been extensively investigated using a variety of experimental techniques, making the vancomycin-peptide complex an ideal model system for the development of new approaches for understanding biomolecular recognition processes. [2][3][4][5][6][7][8][9][10] N-acetyl-D-Ala-D-Ala (AcDADA) and N R ,N -diacetyl-L-Lys-D-Ala-D-Ala (Ac 2 KDADA) shown in Figure 2 are commonly used to mimic cell-wall receptors.…”

“…Detailed understanding of the mechanism of action of glycopeptide antibiotics is important for the development of new agents necessary to overcome the emerging bacterial resistance to vancomycin. It is known that vancomycin prevents the growth of the bacterial cell wall by binding to the cell-wall peptidoglycan precursors terminating in - l -Lys- d -Ala- d -Ala. – Molecular recognition between vancomycin and - d -Ala- d -Ala containing peptide ligands has been extensively investigated using a variety of experimental techniques, making the vancomycin−peptide complex an ideal model system for the development of new approaches for understanding biomolecular recognition processes. – N -acetyl- d -Ala- d -Ala (Ac d A d A) and N α , N ϵ -diacetyl- l -Lys- d -Ala- d -Ala (Ac 2 K d A d A) shown in Figure are commonly used to mimic cell-wall receptors.…”

Affinity in Electrophoresis

“…In its lifetime a substantial number of papers and reviews dealing with affinity interactions in electrophoretic techniques have been published in Electrophoresis (Table 1). More than 125 papers 18, 38, 46, 47, 49–53, 69–71, 93, 101, 110, 118, 129–238 with the word affinity in the title and dealing with some aspect of affinity electrophoresis have been published in the journal since 1989, the year it started being indexed in PubMed. Prior to that, i.e.…”