Gleixner, Jakob and Gattor, Albert O. and Humphrys, Laura J. and Brunner, Thomas and Keller, Max (2023) [<SUP>3</SUP>H]UR-JG102-A Radiolabeled Cyclic Peptide with High Affinity and Excellent Selectivity for the Neuropeptide Y Y<sub>4</sub> Receptor. JOURNAL OF MEDICINAL CHEMISTRY, 66 (19). pp. 13788-13808. ISSN 0022-2623, 1520-4804
Full text not available from this repository. (Request a copy)Abstract
The family of human neuropeptide Y receptors (YRs) comprises four subtypes (Y1R, Y2R, Y4R, and Y5R) that are involved in the regulation of numerous physiological processes. Until now, Y4R binding studies have been predominantly performed in hypotonic sodium-free buffers using I-125-labeled derivatives of the endogenous YR agonists pancreatic polypeptide or peptide YY. A few tritium-labeled Y4R ligands have been reported; however, when used in buffers containing sodium at a physiological concentration, their Y4R affinities are insufficient. Based on the cyclic hexapeptide UR-AK86C, we developed a new tritium-labeled Y4R radioligand ([H-3]UR-JG102, [H-3]20). In sodium-free buffer, [H-3]20 exhibits a very low Y4R dissociation constant (K-d 0.012 nM). In sodium-containing buffer (137 mM Na+), the Y4R affinity is lower (K-d 0.11 nM) but still considerably higher compared to previously reported tritiated Y4R ligands. Therefore, [H-3]20 represents a useful tool compound for the determination of Y4R binding affinities under physiological-like conditions.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | PANCREATIC-POLYPEPTIDE; CARBAMOYLATED ARGININE; FUNCTIONAL EXPRESSION; ALLOSTERIC SODIUM; AMINO ACIDS; FOOD-INTAKE; CLONED RAT; FLUORESCENT; ANTAGONISTS; LIGANDS; |
| Subjects: | 600 Technology > 615 Pharmacy |
| Divisions: | Chemistry and Pharmacy > Institute of Pharmacy |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 09 Mar 2024 09:00 |
| Last Modified: | 09 Mar 2024 09:00 |
| URI: | https://pred.uni-regensburg.de/id/eprint/59249 |
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