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- W2022962561 abstract "The side-chain to side-chain cyclized opioid peptide analogs Orn‐Phe‐A⎵sp‐NH2 (I) and H‐Tyr‐D‐Lys‐Phe‐G⎵lu‐NH2 (II) were synthesized and tested in the guinea pig ileum and mouse vas deferens assays and in binding assays based on displacement of μ- and δ-opioid receptor-selective radioligands from rat brain membranes. The more rigid cyclic analog I containing a 13-membered ring structure showed very high preference for μ-receptors over δ-receptors, whereas the more flexible cyclic peptide II (15-membered ring) was non-selective. These results indicate that variation in the degree of conformational restriction of opioid peptides can produce drastic shifts in their receptor selectivity profile. Because of its high μ-receptor selectivity and rigidity cyclic analog I will be useful for determining the conformational requirements of μ-opioid receptors." @default.
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- W2022962561 title "A novel cyclic opioid peptide analog showing high preference for μ-receptors" @default.
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- W2022962561 doi "https://doi.org/10.1016/s0006-291x(85)80196-0" @default.
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