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- W2079512085 abstract "The cyclic enkephalin analog H-Tyr-D-L-ys-Gly-Phe-Glu-NH2 (I) and the structurally related open chain analogs H-Tyr-D-Nle-Gly-Phe-Gln-NH2 (II) and H-Tyr-D-Lys(For)-Gly-Phe-Abu-NH2 (III) were tested in μ and δ opioid receptor-representative binding assays and bioassays. Whereas both linear analogs showed a pronounced preference for μ receptors over δ receptors, the conformationally restricted cyclic peptide I was found to be unselective. This finding represents the first reported example of a peptide cyclization resulting in a loss of receptor selectivity. From this and earlier studies, it was concluded that the receptor selectivity of cyclized peptide analogs relative to that of their linear correlates may depend on the size and relative rigidity of their ring structures." @default.
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- W2079512085 date "2009-01-12" @default.
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- W2079512085 title "Side chain to side chain cyclization of an enkephalin analog results in loss of opioid receptor selectivity" @default.
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- W2079512085 doi "https://doi.org/10.1111/j.1399-3011.1986.tb03283.x" @default.
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