Anthranilic acid based CCK1 receptor antagonists and CCK-8 have a common step in their "receptor desmodynamic processes"

  • J Med Chem. 2006 Apr 20;49(8):2456-62. doi: 10.1021/jm051050n.
Stefania De Luca  1 ,  Michele Saviano ,  Lucia Lassiani ,  Konstantina Yannakopoulou ,  Penny Stefanidou ,  Luigi Aloj ,  Giancarlo Morelli ,  Antonio Varnavas
Affiliations
  • 1. Interuniversity 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.
PMID: 16610788 DOI: 10.1021/jm051050n
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.