Opioid binding profile of morphiceptin, Tyr-MIF-1 and dynorphin- related peptides in rat brain membranes

N. Sartania, S. Benyhe, A. Magyar, A. Z. Rónai, K. Medzihradszky, A. Borsodi

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

Opioid properties of several morphiceptin- (Tyr-Pro-Phe-Pro-NH2), Tyr- MIF-1 (Tyr-Pro-Leu-Gly-NH2) and dynorphin-derivatives were characterized in rat brain in vitro receptor binding assay and in electrically stimulated longitudinal muscle strip preparation of guinea pig ileum. In the case of morphiceptin-related peptides, an excellent correlation was found between the [3H]-naloxone binding displacement data and the agonist potencies determined in the bioassay. The 'turning point' was the C-terminal amidation in the tri- and tetrapeptide pairs in both series. Tyr-MIF-1 derivatives showed weak affinity in the opioid receptor binding assay and none of them had any remarkable effect in the bioassay either as agonist or antagonist. The dynorphin A((1-10))-peptides modified at positions 5 and 8 retained their affinity with Pro5-, Pro8-, and Ala8- substituents, whereas some loss of affinity was observed in the case of Gly8-Dyn A((1-10)).

Original languageEnglish
Pages (from-to)225-230
Number of pages6
JournalNeuropeptides
Volume30
Issue number3
DOIs
Publication statusPublished - Jan 1 1996

ASJC Scopus subject areas

  • Endocrinology
  • Neurology
  • Endocrine and Autonomic Systems
  • Cellular and Molecular Neuroscience

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