Studies on the interaction of the antibiotic moenomycin A with the enzyme penicillin-binding protein 1b

Bioorg Med Chem. 2003 Jul 3;11(13):2965-81. doi: 10.1016/s0968-0896(03)00187-1.

Abstract

The interaction of a moenomycin derivative with the enzyme penicillin binding protein 1b (PBP 1b) has been studied by means of STD NMR. The results obtained initiated the synthesis of a number of moenomycin derivatives modified in unit A including a moenomycin-ampicillin conjugate and determination of their antibiotic activities. A protocol is described that allows studying the interaction of moenomycin analogues with PBP 1b by fluorescence correlation spectroscopy.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anti-Bacterial Agents / chemical synthesis*
  • Anti-Bacterial Agents / pharmacology
  • Bacterial Proteins / antagonists & inhibitors*
  • Bambermycins / chemical synthesis
  • Bambermycins / pharmacology*
  • Carrier Proteins / antagonists & inhibitors*
  • Diffusion
  • Hexosyltransferases / antagonists & inhibitors*
  • Microbial Sensitivity Tests
  • Muramoylpentapeptide Carboxypeptidase / antagonists & inhibitors*
  • Nuclear Magnetic Resonance, Biomolecular / methods
  • Octoxynol
  • Penicillin-Binding Proteins
  • Peptidyl Transferases / antagonists & inhibitors*
  • Protein Binding
  • Spectrometry, Fluorescence

Substances

  • Anti-Bacterial Agents
  • Bacterial Proteins
  • Carrier Proteins
  • Penicillin-Binding Proteins
  • Bambermycins
  • moenomycin A
  • Octoxynol
  • Peptidyl Transferases
  • Hexosyltransferases
  • Muramoylpentapeptide Carboxypeptidase