In vitro inhibition of human erythrocyte glutathione reductase by some new organic nitrates

Bioorg Med Chem Lett. 2009 Jul 1;19(13):3661-3. doi: 10.1016/j.bmcl.2009.04.087. Epub 2009 Apr 24.


Glutathione reductase (GR), is responsible for the existence of GSH molecule, a crucial antioxidant against oxidative stress reagents. The antimalarial activities of some redox active compounds are attributed to their inhibition of antioxidant flavoenzyme glutathione reductase, and inhibitors are therefore expected to be useful for the treatment of malaria. Twelve organic nitrate derivatives were synthesized and treated with human erythrocyte GR. The molecules were identified as strong GR inhibitors and novel antimalaria candidates.

MeSH terms

  • Antimalarials / chemical synthesis
  • Antimalarials / chemistry*
  • Antimalarials / pharmacology
  • Enzyme Inhibitors / chemical synthesis
  • Enzyme Inhibitors / chemistry*
  • Enzyme Inhibitors / pharmacology
  • Erythrocytes / enzymology*
  • Glutathione Reductase / antagonists & inhibitors*
  • Glutathione Reductase / metabolism
  • Humans
  • Nitrates / chemical synthesis
  • Nitrates / chemistry*
  • Nitrates / pharmacology


  • Antimalarials
  • Enzyme Inhibitors
  • Nitrates
  • Glutathione Reductase