An NMR study of the interaction between the antibiotic ristocetin A and a cell wall peptide analog. Negative nuclear Overhauser effects in the investigation of drug binding sites

Study of mechanisms of chiral discrimination of amino acids and their derivatives on a teicoplanin-based chiral stationary phase

“…COO − represents the most important moiety through which amino acids can interact with the aglycone basket via hydrogen bonding. This has been demonstrated via NMR investigations [18,[47][48][49][50] and, more recently, by X-ray cristallography (although, in that case, for vancomycin macrocyclic antibiotic) [51][52][53]. In particular, Williams et al [16] proposed that, in the binding of acetylated dipeptides to macrocyclic antibiotics, a possible reaction mechanism would include the following steps: (1) binding of the carboxylate anion of the C-terminal amino acid in the pocket of the three amide NH groups of residues 2-4 of the antibiotic (see Fig.…”

Highlighting the role of the chlorine substituents in the glycopeptide antibiotic balhimycin for chiral recognition in capillary electrophoresis

“…It has been established for a long time that antibiotic activity of the vancomycin-type glycopeptide antibiotics rests on the high specificity of the aglycon cavity formed by cyclization of five aromatic side-chains towards the N-acetyl-D-Ala-D-Ala-peptide motif of bacterial cell-wall precursors [27,28]. The molecular bases for this binding are five hydrogen bonds, which have been extensively studied by (NMR) [28][29][30][31] and X-ray crystallography [32][33][34][35][36].…”

“…It has been established for a long time that antibiotic activity of the vancomycin-type glycopeptide antibiotics rests on the high specificity of the aglycon cavity formed by cyclization of five aromatic side-chains towards the N-acetyl-D-Ala-D-Ala-peptide motif of bacterial cell-wall precursors [27,28]. The molecular bases for this binding are five hydrogen bonds, which have been extensively studied by (NMR) [28][29][30][31] and X-ray crystallography [32][33][34][35][36]. Three types of interactions between vancomycin-type antibiotics and D-Ala-D-Ala-terminating peptides have recently been confirmed: (1) the binding of the C-terminal carboxy- late of the D-Ala to the three-amide NH groups of the residues 2-4 of the peptide backbone; (2) the formation of two amide-amide hydrogen bonds between the N-Ac-DAla-D-Ala and the glycopeptide backbone and (3) the hydrophobic interactions of the alanine methyl residue with the aromatic side-chains of the glycopeptides.…”

Die Vancomycin-Antibiotica und der Kampf gegen resistente Bakterien

“…Dies ist unseres Wissens das erste Mal, daû über intermolekulare NOE-Effekte die Struktur eines bimolekularen Komplexes bestimmt wurde. [11] Solche Bestimmungen wurden in den frühen 80er Jahren für die Bindung von Peptiden mit endständigem -d-Ala-d-Ala an Ristocetin A, [44] Vancomycin [45] und Teicoplanin [46] durchgeführt und bildeten die Grundlage für das Bindungsmodell in Schema 2. Dieses Modell, nach dem das Carboxylatanion des Liganden an drei benachbarte Amidprotonen des Antibioticums bindet, ist vor kurzem röntgenkristallographisch bestätigt worden.…”