Abstract
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.
Publication types
-
Comparative Study
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Animals
-
Binding Sites
-
Brain / metabolism
-
Drug Evaluation, Preclinical
-
Guinea Pigs
-
Ileum / drug effects
-
Ileum / metabolism
-
Indoles / chemistry*
-
Indoles / metabolism
-
Indoles / pharmacology*
-
Indolizines / chemistry*
-
Indolizines / metabolism
-
Indolizines / pharmacology*
-
Inhibitory Concentration 50
-
Magnetic Resonance Spectroscopy
-
Molecular Mimicry
-
Molecular Structure
-
Pancreas / metabolism
-
Peptides / chemistry*
-
Peptides / metabolism*
-
Peptides / pharmacology
-
Rats
-
Receptor, Cholecystokinin A
-
Receptor, Cholecystokinin B
-
Receptors, Cholecystokinin / agonists
-
Receptors, Cholecystokinin / antagonists & inhibitors*
-
Receptors, Cholecystokinin / metabolism*
-
Sincalide / metabolism
Substances
-
2-((benzyloxycarbonyl)amino)-1,3a,4,5,10,10a-hexahydro-4-(1-phenylmethyl-2-carboxyethyl)indolo(3,2-e)indolizine-3(2H)-one
-
Indoles
-
Indolizines
-
Peptides
-
Receptor, Cholecystokinin A
-
Receptor, Cholecystokinin B
-
Receptors, Cholecystokinin
-
Sincalide