Abstract
Conformationally constrained dipeptoid analogues containing the type II′ β-turn mimic (2 S,5 S,11b R)-2-amino-3-oxohexahydroindolizino[8,7- b]indole-5-carboxylate framework in place of the α-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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