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Updated: Apr 13, 2026

Determination of High-affinity Antibody-antigen Binding Kinetics Using Four Biosensor Platforms
Published on: April 17, 2017
Biosensor-based affinities and binding kinetics of small molecule antagonists to the adenosine A(2A) receptor
Elena Segala1, James C Errey1, Cédric Fiez-Vandal1
1Heptares Therapeutics, Biopark, Welwyn Garden City, Hertfordshire AL7 3AX, UK.
Abstract:
The options for investigating solubilised G protein-coupled receptors (GPCRs) by biophysical techniques have long been hampered by their instability. A thermostabilised adenosine A2A receptor expressed in insect cells, purified in detergent and reconstituted into high-density lipoprotein (HDL) particles was immobilised onto a Surface Plasmon Resonance sensor chip. This allowed measurement of affinities and kinetics for A2A antagonists with affinities ranging from 50 pM to almost 2 μM. Compared with other formats, reproduction of affinities, and dissociation and association rate constants are good, reasonable and poor respectively, indicating stabilised receptors in HDL particles are useful for investigating specific aspects of GPCR-ligand interactions.
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