Structure-activity studies of dermorphin. The role of side chains of amino acid residues on the biological activity of dermorphin

Krzysztof Darłak, Zbigniew Grzonka, Pawel Krzaścik, Piotr Janicki, S. Witold Gumułka

Research output: Contribution to journalArticlepeer-review

16 Scopus citations

Abstract

Seventeen analogues of dermorphin were synthesized and bio-assayed to determine the influence of side chains of the individual amino acid residues forming the sequence of dermorphin on the biological activity of this opioid peptide. Syntheses were carried out using solid-phase procedure, and the analogues obtained were purified by gel filtration on Sephadex G-10. Biological activities determined in guinea pig ileum (GPI) and mouse vas deferens (MVD) tests showed that the N-terminal tetrapeptide is responsible for the activity of dermorphin. Substitutions in the C-terminal fragment, particularly in position 5, for other amino acid residues results in substantial differentiation towards μ and δ receptors.

Original languageEnglish (US)
Pages (from-to)687-689
Number of pages3
JournalPeptides
Volume5
Issue number4
DOIs
StatePublished - 1984

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Physiology
  • Endocrinology
  • Cellular and Molecular Neuroscience

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