Methionine enkephalin and isosteric analogues. Part II.: Receptor conformation of methionine enkephalin.
Copyright policy )Methionine enkephalin and isosteric analogues. Part II.: Receptor conformation of methionine enkephalin.
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 -CH2CH2-. 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.
Mice, Ileum, Protein Conformation, Enkephalin, Methionine, Guinea Pigs, Receptors, Opioid, Animals, Endorphins, Enkephalins, In Vitro Techniques, Rats
Mice, Ileum, Protein Conformation, Enkephalin, Methionine, Guinea Pigs, Receptors, Opioid, Animals, Endorphins, Enkephalins, In Vitro Techniques, Rats
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