The synthesis and opioid receptor binding affinities of analogues of dermorphin and its N-terminal tetrapeptide fragment with dibasic acids in position 2

Aleksandra Misicka, Andrzej W. Lipkowski, Jirina Slaninova, Peg Davis, Henry I. Yamamura, Frank Porreca, Victor J. Hruby

Research output: Contribution to journalArticle

4 Scopus citations

Abstract

Analysis of possible μ opioid receptor active conformations for dermorphin suggested that the topographical location of the tyramine moiety of the N-tenninal tyrosine can be simulated with the phenol of tyrosine1 or desamino-tyrosine1 (4-hydroxyphenylpropionic acid) and a basic group located on the side chain of a dibasic acid residue located in position 2. The biological properties of respective analogs with D- or L-arginine, and D- or L-lysine in the position 2 of dermorphin or desaminodermorphin and their N-terminal tetrapeptide fragments, has provided evidence in support of this prediction, and questions the dogma that an N-terminal tyrosine is a necessary element for opioid agonist peptides.

Original languageEnglish (US)
Pages (from-to)1633-1640
Number of pages8
JournalLife Sciences
Volume57
Issue number18
DOIs
StatePublished - Sep 22 1995

Keywords

  • GPI assay
  • MVD assay
  • binding assays
  • dermorphin analogues
  • dibasic amino acids
  • δ opioid receptor
  • μ opioid receptor

ASJC Scopus subject areas

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

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