Conformationally constrained dipeptoid analogues containing the type II' beta-turn mimic (2S,5s,11bR)-2-amino-3-oxohexahydroindolizino[8,7-b]indole-5 -carboxylate framework in place of the alpha-MeTrp residue, show high binding affinity and selectivity for CCK-A receptors, suggesting that a turn-like conformation could contribute to the bioactive conformation at this CCK receptor subtype.
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Highly constrained dipeptoid analogues containing a type II' beta-turn mimic as novel and selective CCK-A receptor ligands.
Bioorg Med Chem Lett
January 1999
Instituto de Química Médica (CSIC), Madrid, Spain.
Conformationally constrained dipeptoid analogues containing the type II' beta-turn mimic (2S,5s,11bR)-2-amino-3-oxohexahydroindolizino[8,7-b]indole-5 -carboxylate framework in place of the alpha-MeTrp residue, show high binding affinity and selectivity for CCK-A receptors, suggesting that a turn-like conformation could contribute to the bioactive conformation at this CCK receptor subtype.
View Article and Find Full Text PDFNovel constrained CCK-B dipeptoid antagonists derived from pipecolic acid.
Bioorg Med Chem Lett
June 1998
Département de Pharmacochimie Moléculaire et Structurale, INSERM U266, CNRS URA D1500, UFR des Sciences Pharmaceutiques et Biologiques, Paris, France.
A new series of 4-substituted pipecolic acid derivatives was prepared and incorporated into dipeptoids. The resulting products behave as moderately potent CCK-B antagonists but their constrained structure and its comparison with structurally related compounds yield valuable information about the conformational requirements for optimal recognition of the CCK-B receptor by antagonists.
View Article and Find Full Text PDFSynthesis and biological properties of new constrained CCK-B antagonists: discrimination of two affinity states of the CCK-B receptor on transfected CHO cells.
J Med Chem
November 1997
Département de Pharmacochimie Moléculaire et Structurale, U266 INSERM-URA D1500, CNRS, UFR des Sciences Pharmaceutiques et Biologiques, Paris, France.
To improve our knowledge of the bioactive conformation of CCK-B antagonists, we have developed a new series of constrained dipeptoids whose synthesis and biochemical properties are reported here. These compounds, of general structure N alpha-[(2-adamantyloxy)carbonyl]-alpha-methyltryptophanyl-(4 -X)-proline, were designed by introducing a cyclization in the structure of the previously described CCK-B/peptoid antagonist RB 210, N-[N-[(2-adamantyloxy)carbonyl]-DL-alpha-methyltryptophanyl] -N-(2-phenylethyl)glycine (Blommaert et al. J.
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