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Highly constrained dipeptoid analogues containing a type II′ β-turn mimic as novel and selective CCK-A receptor ligands

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 co...

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Bibliographic Details
Published in:Bioorganic & medicinal chemistry letters 1999-01, Vol.9 (1), p.43-48
Main Authors: Figuera, Natalia de la, Martín-Martínez, Mercedes, Herranz, Rosario, Teresa García-López, M., Latorre, Miriam, Cenarruzabeitia, Edurne, del Río, Joaquín, González-Muñiz, Rosario
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Language:English
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Summary: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. A turn-like conformation could contribute to the bioactive conformation of dipeptoids at the CCK-A receptor.
ISSN:0960-894X
1464-3405
DOI:10.1016/S0960-894X(98)00677-5