Bacterial transferase MraY inhibitors: synthesis and biological evaluation

Bioorg Med Chem. 2010 Jun 15;18(12):4560-9. doi: 10.1016/j.bmc.2010.04.023. Epub 2010 Apr 13.

Abstract

New inhibitors of the bacterial transferase MraY are described. Their structure is based on an aminoribosyl-O-uridine like scaffold, readily obtained in two key steps. The amino group can be coupled with proline or guanylated. Alternatively, these amino, prolinyl or guanidinyl groups can be introduced through a triazole linker. Biological evaluation of these compounds on MraY from Bacillus subtilis revealed interesting inhibitory activity for both amino compounds.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anti-Bacterial Agents / chemical synthesis*
  • Anti-Bacterial Agents / chemistry
  • Anti-Bacterial Agents / pharmacology
  • Bacillus subtilis / enzymology
  • Bacterial Proteins / antagonists & inhibitors*
  • Bacterial Proteins / metabolism
  • Enzyme Inhibitors / chemical synthesis*
  • Enzyme Inhibitors / chemistry
  • Enzyme Inhibitors / pharmacology
  • Transferases (Other Substituted Phosphate Groups)
  • Transferases / antagonists & inhibitors*
  • Transferases / metabolism
  • Triazoles / chemical synthesis
  • Triazoles / chemistry
  • Triazoles / pharmacology

Substances

  • Anti-Bacterial Agents
  • Bacterial Proteins
  • Enzyme Inhibitors
  • Triazoles
  • Transferases
  • Transferases (Other Substituted Phosphate Groups)
  • mraY protein, Bacteria