Premium
Revealing binding interaction between seven drugs and immobilized β 2 ‐adrenoceptor by high‐performance affinity chromatography using frontal analysis
Author(s) -
Xinfeng Zhao,
Jingjing Huang,
Qian Li,
Lusha Wei,
Jianbin Zheng,
Xiaohui Zheng,
Zijian Li,
Youyi Zhang
Publication year - 2013
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/jmr.2271
Subject(s) - chemistry , dissociation constant , affinity chromatography , terbutaline , chromatography , receptor , radioligand , clenbuterol , hydrogen bond , radioligand assay , stereochemistry , molecule , biochemistry , organic chemistry , enzyme , medicine , asthma
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 β 2 ‐adrenoceptors by frontal analysis using immobilized receptor stationary phase. The dissociation constants ( K d ) were determined to be (3.16 ± 0.09) × 10 −4 M for salbutamol, (4.29 ± 0.12) × 10 −4 M for terbutaline, (6.19 ± 0.16) × 10 −4 M for methoxyphenamine, (2.11 ± 0.07) × 10 −4 M for tulobuterol, (1.82 ± 0.11) × 10 −4 M for fenoterol, (9.75 ± 0.24) × 10 −6 M formoterol, and (9.84 ± 0.26) × 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. Copyright © 2013 John Wiley & Sons, Ltd.