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  • Title: Comparison of mu-, delta- and kappa-receptor binding sites through pharmacologic evaluation of p-nitrophenylalanine analogs of opioid peptides.
    Author: Schiller PW, Nguyen TM, DiMaio J, Lemieux C.
    Journal: Life Sci; 1983; 33 Suppl 1():319-22. PubMed ID: 6319885.
    Abstract:
    For the purpose of comparing the structural requirements of opioid receptor subsites interacting with phenylalanine residues of opioid peptides, analogs containing p-nitrophenylalanine (Phe(pNO2) ) were synthesized and tested in the guinea pig ileum (GPI) and mouse vas deferens (MVD) assay as well as in mu- and delta-receptor selective binding assays. Whereas substitution of Phe(pNO2) in position 4 of the mu-selective analog H-Tyr-c[-N epsilon-D-Lys-Gly-Phe-Leu-] and of the delta-selective analog H-Tyr-D-Ser-Gly-Phe-Leu-Thr-OH produced a significant potency increase in all assays, the corresponding substitution in the kappa-selective dynorphin-(1-13) fragment resulted in a decreased potency in the GPI-assay. These findings suggest that the electronic requirements of the Phe4 binding site at the mu- and delta-receptor are identical, but different from those of the corresponding site at the kappa-receptor. The observation that Phe(pNO2) substitution in position 3 of morphiceptin and dermorphin also produces a drastic potency drop indicates that the Phe3 side-chain of the latter peptides at the mu- and delta-receptor may bind to a site different from that interacting with the Phe4 side-chain of enkephalins.
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