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Journal of Biomolecular Screening
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Development of a Homogeneous High Throughput Fluorescence Polarization Assay for G Protein-Coupled Receptor Binding

Paul H. Lee

Discovery Technologies, Pharmacia & Upjohn, Kalamazoo, MI

Debra J. Bevis

Discovery Technologies, Pharmacia & Upjohn, Kalamazoo, MI

Traditional methods that follow receptor ligand interactions are competitive assays in which the test compound displaces a radiolabeled molecule. These assays require either a time-consuming step for separation of free ligands from bound ligands or immobilization of receptors and the scintillant on a solid-phase support. In this report, we describe the development of a homogeneous binding assay for a G protein-coupled receptor in the fluorescence polarization format. This homogeneous fluorescence polarization binding assay format is superior to the traditional binding methods because no radioisotope, separation step, or solid-phase support is required. The elimination of the separation step enhances detection of low-affinity ligands and enables a real-time, continuous readout of the binding activity in a high throughput 384-well microplate format.

Journal of Biomolecular Screening, Vol. 5, No. 6, 415-419 (2000)
DOI: 10.1177/108705710000500604
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