Gas-phase noncovalent interactions between vancomycin-group antibiotics and bacterial cell-wall precursor peptides probed by hydrogen/deuterium exchange
UNSPECIFIED. (1998) Gas-phase noncovalent interactions between vancomycin-group antibiotics and bacterial cell-wall precursor peptides probed by hydrogen/deuterium exchange. JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY, 9 (12). pp. 1255-1266. ISSN 1044-0305Full text not available from this repository.
Gas-phase structures of noncovalent complexes between the glycopeptide antibiotics vancomycin, eremomycin, ristocetin, and pseudo aglyco-ristocetin acid the cell-wall mimicking peptides N-acetyl-D-Alanyl-D-Alanine, N-acetyl-Glycyl-D-Alanine, and N,N'-di-acetyl L-Lysyl-D-Alanyl-D-Alanine have been probed by hydrogen/deuterium (H/D) exchange using ND, as reagent gas. The noncovalent complexes were transferred from solution to the vacuum using electrospray ionization. The H/D exchange of the solvent-free ions was studied in a Fourier transform ion cyclotron resonance mass spectrometer. The H/D exchange behavior of the free antibiotics and the free peptides were compared with the exchange observed for the antibiotic-peptide complexes. A general increase was found in the degree of deuterium incorporation upon complex formation with the ligand, which indicates that the peptide binding makes more sites on the antibiotic capable of taking part in the H/D exchange. Apart from H/D exchange, adduct formation with ND, was observed, but only for the singly protonated peptides and the doubly protonated [ristocetin + N-acetyl-D-Alanyl-D-Alanine]. This marked difference in chemical reactivity of closely related systems such as [ristocetin+N-acetyl-Glycyl-D-Alanine] and [ristocetin+N-acetyl-D-Alanyl-D-Alanine] indicates that the gas-phase structures of these noncovalent complexes are quite sensitive to small changes in the primary structures of the peptides. The gas-phase structures of the antibiotic-peptide complexes are probably different from the solution-phase structures, with the peptides no longer bound to the characteristic solution-phase binding pockets of the antibiotics. (C) 1998 American Society for Mass Spectrometry.
|Item Type:||Journal Article|
|Subjects:||Q Science > QD Chemistry
Q Science > QC Physics
|Journal or Publication Title:||JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY|
|Publisher:||ELSEVIER SCIENCE INC|
|Number of Pages:||12|
|Page Range:||pp. 1255-1266|
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