Time-Resolved FRET-Based Assays to Characterize G Protein-Coupled Receptor Hetero-oligomer Pharmacology.
Fiche publication
Date publication
janvier 2019
Journal
Methods in molecular biology (Clifton, N.J.)
Auteurs
Membres identifiés du Cancéropôle Est :
Dr BONNET Dominique
Tous les auteurs :
Heuninck J, Hounsou C, Dupuis E, Trinquet E, Mouillac B, Pin JP, Bonnet D, Durroux T
Lien Pubmed
Résumé
Although G protein-coupled receptor (GPCR) oligomerization is a matter of debate, it has been shown that the nature of the GPCR partners within the oligomers can influence the pharmacological properties of the receptors. Therefore, finding specific ligands for homo- or hetero-oligomers opens new perspectives for drug discovery. However, no efficient experimental strategy to screen for such ligands existed yet. Indeed, conventional binding strategies do not discriminate ligand binding on GPCR monomers, homo- or hetero-oligomers. To address this issue, we recently developed a new assay based on a time-resolved FRET method that is easy to implement and that can focus on ligand binding specifically on the hetero-oligomer.
Mots clés
Binding experiment, Fluorescent ligand, G protein-coupled receptor, HTRF®, Homo- and hetero-oligomerization, Lanthanide, Self-labeling enzyme, Tag-lite® screening, Terbium, Time-resolved FRET
Référence
Methods Mol. Biol.. 2019 ;1947:151-168