Stereoselective binding of indomethacin ethanolamide derivatives to cyclooxygenase-1

J Med Chem. 2005 May 19;48(10):3613-20. doi: 10.1021/jm0494164.

Abstract

We have used molecular modeling studies and molecular dynamics simulations to generate three-dimensional models for cyclooxygenase-1 complexes with a series of indomethacin ethanolamide derivatives. These studies provide a plausible explanation for the stereoselective ligand binding preferences observed experimentally for these inhibitors and predict the general binding mode as well as specific structural details for the ligand-enzyme complexes. These studies provide insight into the nature of cyclooxygenase-1 interactions with a series of novel inhibitors and should help increase our understanding of key structural determinants for cyclooxygenase isozyme-selective inhibitor binding.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Binding Sites
  • Cyclooxygenase 1
  • Cyclooxygenase Inhibitors / chemistry*
  • Ethanolamines / chemistry*
  • Hydrogen Bonding
  • Indomethacin / analogs & derivatives*
  • Indomethacin / chemistry*
  • Ligands
  • Models, Molecular
  • Molecular Conformation
  • Prostaglandin-Endoperoxide Synthases / chemistry*
  • Protein Binding
  • Quantitative Structure-Activity Relationship
  • Sheep
  • Stereoisomerism
  • Thermodynamics

Substances

  • Cyclooxygenase Inhibitors
  • Ethanolamines
  • Ligands
  • Cyclooxygenase 1
  • Prostaglandin-Endoperoxide Synthases
  • Indomethacin