Revealing binding interaction between seven drugs and immobilized beta2-adrenoceptor by high-performance affinity chromatography using frontal analysis.

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Citation

Zhao XF, Huang JJ, Li Q, Wei LS, Zheng JB, Zheng XH, Li ZJ, Zhang YY

Revealing binding interaction between seven drugs and immobilized beta2-adrenoceptor by high-performance affinity chromatography using frontal analysis.

J Mol Recognit. 2013 May;26(5):252-7. doi: 10.1002/jmr.2271.

PubMed ID
23526777 [ View in PubMed
]
Abstract

The development of new approaches to study the affinity between ligands and G-protein-coupled receptors proves to be of growing interest for pharmacologists, chemists, and biologists. The aim of this work was to determine the binding of seven drugs to beta2-adrenoceptors by frontal analysis using immobilized receptor stationary phase. The dissociation constants (Kd ) were determined to be (3.16 +/- 0.09) x 10(-4) M for salbutamol, (4.29 +/- 0.12) x 10(-4) M for terbutaline, (6.19 +/- 0.16) x 10(-4) M for methoxyphenamine, (2.11 +/- 0.07) x 10(-4) M for tulobuterol, (1.82 +/- 0.11) x 10(-4) M for fenoterol, (9.75 +/- 0.24) x 10(-6) M formoterol, and (9.84 +/- 0.26) x 10(-5) M for clenbuterol. These results showed a good correlation with the data determined by radioligand binding assay. Further investigations revealed that the dissociation constant mainly attributed to the number of hydrogen bonds in the structures of ligands. This study indicates that affinity chromatography using immobilized receptor stationary phase can be used for the direct determination of drug-receptor binding interactions and has the potential to become a reliable alternative for quantitative studies of ligand-receptor interactions.

DrugBank Data that Cites this Article

Drug Targets
DrugTargetKindOrganismPharmacological ActionActions
TulobuterolBeta-2 adrenergic receptorProteinHumans
Unknown
Regulator
Details