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An attempt to structurally convert mu-selective morphine toward delta-receptor binding: dimerization based on enkephalin conformation.

H Yara·Y Katagawa·M Doi·T Ishida·M Inoue·M Yasuda·A Baba·H Iwata·K Kitamura·T Sadatome
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Abstract

In order to elucidate the substrate specificities for mu- and delta-opioid receptors, dimerization of the mu-specific morphine molecule was attempted, based on the hypothesis of the possible relationship between the molecular conformation of endogenous enkephalin and its selectivity for each opioid receptor. The NOR2 ([normorphine]N-CH2-CH2-N[normorphine]) thus synthesized exhibited agonist activity showing a preference for binding with the delta-opioid receptor, compared with the parent morphine molecule. Antagonist activity was also observed for NOR3 ([normorphine]N-CH2-CH2-CH2-N[normorphine]).

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AnimalsBinding, CompetitiveBrainChemical PhenomenaChemistry, PhysicalEnkephalin, Ala(2)-MePhe(4)-Gly(5)-Enkephalin, D-Penicillamine (2,5)-EnkephalinsIn Vitro TechniquesMaleMiceMorphineMorphine DerivativesMuscle ContractionMuscle, SmoothProtein ConformationRatsRats, Inbred StrainsReceptors, OpioidReceptors, Opioid, deltaReceptors, Opioid, kappaReceptors, Opioid, muVas DeferensJournal ArticleResearch Support, Non-U.S. Gov't

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BibTeXRIS

H Yara, Y Katagawa, M Doi, T Ishida, M Inoue, M Yasuda, A Baba, H Iwata, K Kitamura, T Sadatome. 1990-06-12. An attempt to structurally convert mu-selective morphine toward delta-receptor binding: dimerization based on enkephalin conformation.. https://doi.org/10.1016/0922-4106(90)90196-5

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