sincalide and anthranilic-acid

sincalide has been researched along with anthranilic-acid* in 2 studies

Other Studies

2 other study(ies) available for sincalide and anthranilic-acid

Article	Year
New anthranilic acid based antagonists with high affinity and selectivity for the human cholecystokinin receptor 1 (hCCK1-R). Journal of medicinal chemistry, 2011, Aug-25, Volume: 54, Issue:16 The anthranilic acid diamides represent the most recent class of nonpeptide CCK(1) receptor (CCK(1)-R) antagonists. Herein we describe the second phase of the anthranilic acid C-terminal optimization using nonproteinogenic amino acids containing a phenyl ring in their side chain. The Homo-Phe derivative 2 (VL-0797) enhanced 12-fold the affinity for the rat CCK(1)-R affinity and 15-fold for the human CCK(1)-R relative to the reference compound 12 (VL-0395). The eutomer of 2 (6) exhibited a nanomolar range affinity toward the human CCK(1)-R and was at least 400-fold selective for the CCK(1)-R over the CCK(2)-R. Molecular docking in the modeled CCK(1)-R and its validation by site-directed mutagenesis experiments showed that the 6 binding site overlaps that occupied by the C-terminal bioactive region of the natural agonist CCK. Owing to their interesting properties, new compounds provided by this study represent a solid basis for further advances aimed at synthesis of clinically valuable CCK(1)-R antagonists. Topics: Aminobutyrates; Animals; Binding Sites; Binding, Competitive; Cerebral Cortex; Chlorocebus aethiops; COS Cells; Gallbladder; Guinea Pigs; Heterocyclic Compounds; Humans; In Vitro Techniques; Indoles; Male; Models, Molecular; Molecular Structure; Muscle Contraction; Mutagenesis, Site-Directed; Mutation; ortho-Aminobenzoates; Pancreas; Rats; Rats, Sprague-Dawley; Receptor, Cholecystokinin A; Sincalide; Structure-Activity Relationship	2011
Anthranilic acid based CCK1 receptor antagonists and CCK-8 have a common step in their "receptor desmodynamic processes". Journal of medicinal chemistry, 2006, Apr-20, Volume: 49, Issue:8 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. Topics: Animals; Binding, Competitive; Biological Assay; Humans; Indoles; Ligands; Magnetic Resonance Spectroscopy; Models, Molecular; Molecular Structure; ortho-Aminobenzoates; Pancreas; Proglumide; Protein Conformation; Rats; Receptor, Cholecystokinin A; Sincalide; Spectrometry, Fluorescence; Structure-Activity Relationship	2006

Article

Year

New anthranilic acid based antagonists with high affinity and selectivity for the human cholecystokinin receptor 1 (hCCK1-R).

Journal of medicinal chemistry, 2011, Aug-25, Volume: 54, Issue:16

The anthranilic acid diamides represent the most recent class of nonpeptide CCK(1) receptor (CCK(1)-R) antagonists. Herein we describe the second phase of the anthranilic acid C-terminal optimization using nonproteinogenic amino acids containing a phenyl ring in their side chain. The Homo-Phe derivative 2 (VL-0797) enhanced 12-fold the affinity for the rat CCK(1)-R affinity and 15-fold for the human CCK(1)-R relative to the reference compound 12 (VL-0395). The eutomer of 2 (6) exhibited a nanomolar range affinity toward the human CCK(1)-R and was at least 400-fold selective for the CCK(1)-R over the CCK(2)-R. Molecular docking in the modeled CCK(1)-R and its validation by site-directed mutagenesis experiments showed that the 6 binding site overlaps that occupied by the C-terminal bioactive region of the natural agonist CCK. Owing to their interesting properties, new compounds provided by this study represent a solid basis for further advances aimed at synthesis of clinically valuable CCK(1)-R antagonists.

Topics: Aminobutyrates; Animals; Binding Sites; Binding, Competitive; Cerebral Cortex; Chlorocebus aethiops; COS Cells; Gallbladder; Guinea Pigs; Heterocyclic Compounds; Humans; In Vitro Techniques; Indoles; Male; Models, Molecular; Molecular Structure; Muscle Contraction; Mutagenesis, Site-Directed; Mutation; ortho-Aminobenzoates; Pancreas; Rats; Rats, Sprague-Dawley; Receptor, Cholecystokinin A; Sincalide; Structure-Activity Relationship

2011

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

Journal of medicinal chemistry, 2006, Apr-20, Volume: 49, Issue:8

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.

Topics: Animals; Binding, Competitive; Biological Assay; Humans; Indoles; Ligands; Magnetic Resonance Spectroscopy; Models, Molecular; Molecular Structure; ortho-Aminobenzoates; Pancreas; Proglumide; Protein Conformation; Rats; Receptor, Cholecystokinin A; Sincalide; Spectrometry, Fluorescence; Structure-Activity Relationship

2006