Structurally diversified heterocycles and related privileged scaffolds as potential urease inhibitors: a brief overview

Arch Pharm (Weinheim). 2013 Jun;346(6):423-46. doi: 10.1002/ardp.201300041. Epub 2013 May 28.

Abstract

Ureases have emerged as significant virulence factors implicated in the pathogenesis of many clinical conditions such as pyelonephritis, hepatic coma, peptic ulceration, and the formation of injection-induced urinary stones and stomach cancer. They have also been identified as important targets in research both for human and animal health, as well as in agriculture. Strategies based on urease inhibition are the main treatment of diseases caused by urease-producing bacteria. So, in the present context, a diverse library of chemical structures is known to possess remarkable inhibitory activities against urease enzymes. The current review article summarizes and discusses endeavours towards the developments in the burgeoning field of urease inhibition in medicinal chemistry, with an emphasis on the insights that have been gleaned into the structural features that contribute to high and promising levels of anti-urease activity.

Publication types

  • Review

MeSH terms

  • Animals
  • Drug Design
  • Enzyme Inhibitors / chemistry
  • Enzyme Inhibitors / pharmacology*
  • Heterocyclic Compounds / chemistry
  • Heterocyclic Compounds / pharmacology*
  • Humans
  • Small Molecule Libraries
  • Structure-Activity Relationship
  • Urease / antagonists & inhibitors*
  • Urease / metabolism

Substances

  • Enzyme Inhibitors
  • Heterocyclic Compounds
  • Small Molecule Libraries
  • Urease