Structure-activity relationships of pyrrole based S-nitrosoglutathione reductase inhibitors: pyrrole regioisomers and propionic acid replacement

Bioorg Med Chem Lett. 2011 Jun 15;21(12):3671-5. doi: 10.1016/j.bmcl.2011.04.086. Epub 2011 Apr 24.

Abstract

S-Nitrosoglutathione reductase (GSNOR) is a member of the alcohol dehydrogenase family (ADH) that regulates the levels of S-nitrosothiols (SNOs) through catabolism of S-nitrosoglutathione (GSNO). GSNO and SNOs are implicated in the pathogenesis of many diseases including those in respiratory, cardiovascular, and gastrointestinal systems. The pyrrole based N6022 was recently identified as a potent, selective, reversible, and efficacious GSNOR inhibitor which is currently undergoing clinical development. We describe here the synthesis and structure-activity relationships (SAR) of novel pyrrole based analogues of N6022 focusing on scaffold modification and propionic acid replacement. We identified equally potent and novel GSNOR inhibitors having pyrrole regioisomers as scaffolds using a structure based approach.

MeSH terms

  • Aldehyde Oxidoreductases / antagonists & inhibitors*
  • Benzamides / chemical synthesis
  • Benzamides / chemistry*
  • Benzamides / pharmacology*
  • Enzyme Activation / drug effects
  • Enzyme Inhibitors / chemical synthesis
  • Enzyme Inhibitors / chemistry*
  • Enzyme Inhibitors / pharmacology*
  • Inhibitory Concentration 50
  • Molecular Structure
  • Propionates / chemical synthesis
  • Propionates / chemistry*
  • Propionates / pharmacology*
  • Pyrroles / chemical synthesis
  • Pyrroles / chemistry*
  • Pyrroles / pharmacology*
  • Stereoisomerism
  • Structure-Activity Relationship

Substances

  • Benzamides
  • Enzyme Inhibitors
  • N6022
  • Propionates
  • Pyrroles
  • Aldehyde Oxidoreductases
  • formaldehyde dehydrogenase, glutathione-independent
  • propionic acid