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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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Published in: | Bioorganic & medicinal chemistry letters 1999-01, Vol.9 (1), p.43-48 |
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Main Authors: | , , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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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. |
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ISSN: | 0960-894X 1464-3405 |
DOI: | 10.1016/S0960-894X(98)00677-5 |