C-Terminal properties are important for ring-fused 2-pyridones that interfere with the chaperone function in uropathogenic E. coli

Org Biomol Chem. 2005 Nov 7;3(21):3886-92. doi: 10.1039/b509376g. Epub 2005 Sep 5.

Abstract

Virulence-associated organelles, termed pili or fimbriae, are assembled via the highly conserved chaperone-usher pathway in a vast number of pathogenic bacteria. Substituted bicyclic 2-pyridones, pilicides, inhibit pilus formation, possibly by interfering with the active site residues Arg8 and Lys112 of chaperones in uropathogenic E. coli. In this article we describe the synthesis and evaluation of nine analogues of a biologically active pilicide. Derivatization was performed with respect to its C-terminal features and the affinities for the chaperone PapD were studied with 1H relaxation-edited NMR spectroscopy. It could be concluded that the carboxylic acid functionality and also its spatial location was important for binding. In all cases, binding was significantly reduced or even abolished when the carboxylic acid was replaced by other substituents. In addition, in vivo results from a hemagglutination assay are presented where the derivatives have been evaluated for their ability to inhibit pilus formation in uropathogenic E. coli.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anti-Bacterial Agents / chemistry*
  • Anti-Bacterial Agents / pharmacology
  • Escherichia coli / pathogenicity
  • Escherichia coli Proteins / drug effects
  • Fimbriae, Bacterial / drug effects
  • Hemagglutination
  • Magnetic Resonance Spectroscopy
  • Microbial Sensitivity Tests
  • Molecular Chaperones / drug effects*
  • Periplasmic Proteins / drug effects
  • Pyridones / chemical synthesis*
  • Pyridones / pharmacology*
  • Structure-Activity Relationship

Substances

  • Anti-Bacterial Agents
  • Escherichia coli Proteins
  • Molecular Chaperones
  • PapD protein, E coli
  • Periplasmic Proteins
  • Pyridones