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Updated: Aug 9, 2026

A "Dual-Addition" Calcium Fluorescence Assay for the High-Throughput Screening of Recombinant G Protein-Coupled Receptors
Published on: December 2, 2022
Anthranilic acid based CCK1 receptor antagonists and CCK-8 have a common step in their "receptor desmodynamic
Stefania De Luca1, Michele Saviano, Lucia Lassiani
1Interuniversity Research Center on Bioactive Peptides (CIRPeB), University of Naples Federico II, and Institute of Biostructures and Bioimaging of CNR, Via Mezzocannone, 16 I-80134 Naples, Italy.
Abstract:
The interaction between the 1-47 N-terminus of the CCK(1)-R and the anthranilic acid based antagonists has been investigated by fluorescence spectroscopy. These antagonists interact with W39 of the N-terminal domain of the CCK(1)-R like that of the endogenous ligand CCK-8. This specific interaction was not found in other nonpeptide ligands of the CCK(1)-R. Conformational studies, using NMR and energy minimization procedures, have allowed formulation of a new hypothesis on the CCK(1)-R binding mode of the anthranilic antagonists.
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