Bacterial transferase MraY inhibitors: synthesis and biological evaluation.

Bioorg Med Chem

Université Paris Descartes, UMR 8601 CNRS, Laboratoire de Chimie et Biochimie Pharmacologiques et Toxicologiques, 75006 Paris, France.

Published: June 2010

AI Article Synopsis

  • New inhibitors targeting the bacterial enzyme MraY have been developed using a specific structural framework inspired by aminoribosyl-O-uridine.
  • These compounds can be synthesized efficiently in just two key steps, with modifications possible using amino, proline, or guanidine groups through direct coupling or a triazole linker.
  • Tests on Bacillus subtilis show that these newly synthesized amino compounds exhibit significant inhibitory effects on MraY activity.

Article 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.

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Source
http://dx.doi.org/10.1016/j.bmc.2010.04.023DOI Listing

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