Rational approaches towards reversible inhibition of type B monoamine oxidase. Design and evaluation of a novel 5H-Indeno[1,2-c]pyridazin-5-one derivative

Bioorg Med Chem Lett. 2003 Jan 6;13(1):69-73. doi: 10.1016/s0960-894x(02)00838-7.

Abstract

The stereoelectronic properties of several potent reversible monoamine oxidase B (MAO-B) inhibitors were studied with a view to develop a pharmacophore model for reversible MAO-B inhibition. This study suggested that important specific H-bond and hydrophobic interactions are required for potent and selective MAO-B inhibition. These requirements were applied in the design and synthesis of a novel reversible and selective MAO-B inhibitor, 3-methyl-8-(4,4,4-trifluoro-butoxy)indeno[1,2-c]pyridazin-5-one, that is ca. 7000 times more selective as an inhibitor for MAO-B than for MAO-A, with K(i(MAO-B)) in the low nanomolar range.

MeSH terms

  • Drug Design
  • Humans
  • Hydrogen Bonding
  • Hydrophobic and Hydrophilic Interactions
  • Inhibitory Concentration 50
  • Kinetics
  • Models, Molecular
  • Monoamine Oxidase / chemistry*
  • Monoamine Oxidase / metabolism
  • Monoamine Oxidase Inhibitors / chemical synthesis*
  • Monoamine Oxidase Inhibitors / pharmacology
  • Pyridazines / chemical synthesis*
  • Pyridazines / pharmacology
  • Structure-Activity Relationship

Substances

  • Monoamine Oxidase Inhibitors
  • Pyridazines
  • Monoamine Oxidase