Design, synthesis, and biological testing of potential heme-coordinating nitric oxide synthase inhibitors

Bioorg Med Chem. 2006 May 1;14(9):3185-98. doi: 10.1016/j.bmc.2005.12.043. Epub 2006 Jan 20.

Abstract

Based on computer modeling of the active site of nitric oxide synthases (NOS), a series of 10 amidine compounds (9-18) was designed including potential inhibitors that involve the coordination of side-chain functional groups with the iron of the heme cofactor. The most potent and selective compound was the methylthio amidine analogue 9, which was more potent than L-nitroarginine with 185-fold selectivity for inhibition of neuronal NOS over endothelial NOS. It also exhibited time-dependent inhibition, but did not involve the mechanism previously proposed for other amidine inhibitors of NOS. None of the compounds, however, exhibited heme-binding characteristics according to absorption spectroscopy.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Animals
  • Arginine / analogs & derivatives
  • Arginine / chemistry
  • Arginine / pharmacology
  • Chromatography, High Pressure Liquid
  • Computer Simulation
  • Drug Design*
  • Enzyme Inhibitors / chemical synthesis
  • Enzyme Inhibitors / chemistry
  • Enzyme Inhibitors / pharmacology
  • Heme / chemistry*
  • Heme / metabolism*
  • Inhibitory Concentration 50
  • Mice
  • Molecular Structure
  • Nitric Oxide Synthase / antagonists & inhibitors*
  • Nitric Oxide Synthase / pharmacology*
  • Rats
  • Spectrum Analysis
  • Structure-Activity Relationship
  • Substrate Specificity

Substances

  • Enzyme Inhibitors
  • Heme
  • Arginine
  • Nitric Oxide Synthase