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- W1964096605 abstract "Biological activities are reported for two different types of analogues of methionine enkephalin. Cyclic analogues, bridged between the amino- and carboxy- terminals of the parent peptide, are inactive. In contrast, significant levels of activity are displayed by linear isosterically modified analogues in which the Tyr1 -Gly2 peptide bond is replaced by either -CH2NH- or -CH2 CH2-. Similar replacements of the Gly2-Gly3 peptide bond yield compounds with much reduced potency. These modifications serve as useful probes of the receptor conformation. Based on these findings, a model is proposed for interaction between enkephalin and its receptor." @default.
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- W1964096605 date "2009-01-12" @default.
- W1964096605 modified "2023-09-26" @default.
- W1964096605 title "METHIONINE ENKEPHALIN AND ISOSTERIC ANALOGUES" @default.
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- W1964096605 doi "https://doi.org/10.1111/j.1399-3011.1980.tb02558.x" @default.
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