Highly constrained dipeptoid analogues containing a type II' beta-turn mimic as novel and selective CCK-A receptor ligands.

@article{Figuera1999HighlyCD,
  title={Highly constrained dipeptoid analogues containing a type II' beta-turn mimic as novel and selective CCK-A receptor ligands.},
  author={N. de la Figuera and M. Mart{\'i}n-Mart{\'i}nez and R. Herranz and M. Garc{\'i}a-L{\'o}pez and M. Latorre and E. Cenarruzabeitia and J. del R{\'i}o and R. Gonz{\'a}lez-Mu{\~n}iz},
  journal={Bioorganic \& medicinal chemistry letters},
  year={1999},
  volume={9 1},
  pages={
          43-8
        }
}
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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Topics from this paper

29 – DESIGN OF PEPTIDOMIMETICS
Moleular models for cholecystokinin-A receptor.
Cholecystokinin antagonists: Pharmacological and therapeutic potential
  • R. Herranz
  • Biology, Medicine
  • Medicinal research reviews
  • 2003

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