New opioid affinity labels containing maleoyl moiety

Ildikó Szatmári, György Orosz, András Z. Rónai, Éva Makó, Kálmán Medzihradszky, Anna Borsodi

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

Opioid receptor binding properties and pharmacological profiles of novel peptides containing maleoyl function were determined in order to develop new affinity labels. Based on the enkephalin structure peptide ligands were synthesized and tested. Both in in vitro receptor binding experiments and pharmacological studies, all ligands showed agonist character with relatively high affinity (K(i) values in the nanomolar range) and good to moderate selectivity. Replacement of Gly2 in the enkephalin frame with D-Ala led to higher affinities with a small decrease in selectivity. The longer peptide chains resulted in compounds with high percentage (up to 86%) of irreversible binding. The selectivity pattern of the ligands is in good agreement with the data obtained from the pharmacological assays (guinea pig ileum and mouse vas deferens bioassays). The newly synthesized peptides could be used in further studies in order to determine more detailed characteristics of the ligand-receptor interaction.

Original languageEnglish
Pages (from-to)1795-1805
Number of pages11
JournalLife Sciences
Volume65
Issue number17
DOIs
Publication statusPublished - Sep 17 1999

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Keywords

  • Affinity labels
  • Ligand binding
  • Maleoyl peptides
  • Opioid receptor

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Pharmacology, Toxicology and Pharmaceutics(all)

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