Enantiomeric resolution of a novel chiral cannabinoid receptor ligand

J Biochem Biophys Methods. 2002 Dec 31;54(1-3):415-22. doi: 10.1016/s0165-022x(02)00144-6.

Abstract

The enantiomeric resolution of a racemic novel cannabinoid receptor ligand conformationally restricted at the southern aliphatic chain was accomplished using a ChiralPak AD column. Both enantiomers were tested for their competitive binding to the rat brain CB1, mouse spleen CB2 and human CB2 receptors. The levorotatory isomer showed exceptionally high affinity for the CB1 receptor with a seven-fold selectivity over CB2.

Publication types

  • Evaluation Study
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amylose* / analogs & derivatives*
  • Animals
  • Cannabinoids / analysis*
  • Cannabinoids / chemistry
  • Cannabinoids / classification
  • Cannabinoids / metabolism*
  • Carbamates*
  • Chromatography, High Pressure Liquid / instrumentation
  • Chromatography, High Pressure Liquid / methods*
  • Humans
  • Kidney / embryology
  • Kidney / metabolism
  • Ligands
  • Membranes / metabolism
  • Mice
  • Phenylcarbamates*
  • Prosencephalon / metabolism
  • Protein Binding
  • Rats
  • Receptor, Cannabinoid, CB2*
  • Receptors, Cannabinoid
  • Receptors, Drug / analysis
  • Receptors, Drug / metabolism*
  • Spleen / metabolism
  • Stereoisomerism
  • Synaptosomes / metabolism

Substances

  • Cannabinoids
  • Carbamates
  • Cnr2 protein, rat
  • Ligands
  • Phenylcarbamates
  • Receptor, Cannabinoid, CB2
  • Receptors, Cannabinoid
  • Receptors, Drug
  • Chiralpak AD
  • Amylose