Design and structural analysis of aromatic inhibitors of type II dehydroquinase from Mycobacterium tuberculosis

ChemMedChem. 2015 Jan;10(1):116-33. doi: 10.1002/cmdc.201402298. Epub 2014 Sep 18.

Abstract

3-Dehydroquinase, the third enzyme in the shikimate pathway, is a potential target for drugs against tuberculosis. Whilst a number of potent inhibitors of the Mycobacterium tuberculosis enzyme based on a 3-dehydroquinate core have been identified, they generally show little or no in vivo activity, and were synthetically complex to prepare. This report describes studies to develop tractable and drug-like aromatic analogues of the most potent inhibitors. A range of carbon-carbon linked biaryl analogues were prepared to investigate the effect of hydrogen bond acceptor and donor patterns on inhibition. These exhibited inhibitory activity in the high-micromolar range. The addition of flexible linkers in the compounds led to the identification of more potent 3-nitrobenzylgallate- and 5-aminoisophthalate-based analogues.

Keywords: Mycobacterium tuberculosis; dehydroquinase; drug design; inhibitors; protein structures.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / antagonists & inhibitors*
  • Bacterial Proteins / metabolism
  • Binding Sites
  • Catalytic Domain
  • Crystallography, X-Ray
  • Drug Design*
  • Enzyme Inhibitors / chemical synthesis
  • Enzyme Inhibitors / chemistry*
  • Enzyme Inhibitors / pharmacology
  • Hydro-Lyases / antagonists & inhibitors*
  • Hydro-Lyases / metabolism
  • Isonicotinic Acids / chemical synthesis
  • Isonicotinic Acids / chemistry
  • Isonicotinic Acids / pharmacology
  • Molecular Dynamics Simulation
  • Mycobacterium tuberculosis / drug effects
  • Mycobacterium tuberculosis / enzymology*
  • Shikimic Acid / chemistry
  • Structure-Activity Relationship

Substances

  • Bacterial Proteins
  • Enzyme Inhibitors
  • Isonicotinic Acids
  • Shikimic Acid
  • Hydro-Lyases
  • 3-dehydroquinate dehydratase
  • citrazinic acid