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Receptor Binding Assays using Fluorescence Polarization Detection: the [FP]2TM Characterized Tracers

tant for a particular fluorophore, regardless of whether it is free in solution, derivatized to a peptide or, while covalently attached to that peptide, also bound to a receptor, one can differentiate between the three states by the extent of rotation that occurs over this time. The greater the rotation, the greater the depolarization of the excitation light leading to a smaller polarization signal.

In the case of a fluorescent derivative of a peptide bound to a GPCR embedded in a cell membrane fragment, little rotation can occur over the fluorescence lifetime since the cell membrane fragment behaves essentially as a solid phase over this period. Thus emission from the fluorophore remains polarized to a large degree (high signal). Conversely, if the derivatized peptide is displaced from the GPCR, as would be the case in the presence of a potent inhibitor to the ligand receptor interaction, significant rotation can occur over the fluorescence lifetime, which translates into a significant depolarization (small signal). In the intermediate cases of partially bound derivatized peptide, the magnitude of the signal is directly proportional to the extent of binding, to a first approximation10,11.

Materials and Methods

All fluorescently labeled peptides listed below in Table 1 are available from PerkinElmer Life Sciences. They are provided as off-the-shelf reagents accompanied by buffer recommendations, which have been optimized to allow for maximum assay performance. All have been tested against commercially available recombinant GPCRs expressed in mammalian cell membrane preparations.

Performance validation of the peptides consisted of verifying appropriate pharmacology by titrating the binding event with known displacers, usually the native peptide, and detecting the concentration-related response with fluorescence polarization detection. In addition to
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