Subtlety of the structure-affinity and structure-efficacy relationships around a nonpeptide oxytocin receptor agonist.
Fiche publication
Date publication
février 2010
Auteurs
Membres identifiés du Cancéropôle Est :
Pr HIBERT Marcel
Tous les auteurs :
Frantz MC, Rodrigo J, Boudier L, Durroux T, Mouillac B, Hibert M
Lien Pubmed
Résumé
Very few nonpeptide oxytocin agonists have currently been reported, and none of them seem suitable for the in vivo investigation of the oxytocin mediated functions. In an attempt to rationalize the design of better tools, we have systematically studied the structural determinants of the affinity and efficacy of representative ligands of the V(1a), V(2), and OT receptor subtypes. Despite apparently obvious similarity between the ligand structures on one hand, and between the receptor subtypes on the other hand, the binding affinity and the functional activity profiles of truncated and hybrid ligands highlight the subtlety of ligand-receptor interactions for obtaining nonpeptide OT receptor agonists.
Référence
J Med Chem. 2010 Feb 25;53(4):1546-62.