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Isolation of dermenkephalin from amphibian skin, a high‐affinity (δ‐selective opioid heptapeptide containing a D‐amino acid residue
Author(s) -
Mor Amram,
Delfour Antoine,
Sagan Sandrine,
Amiche Mohamed,
Pradelles Philippe,
Rossier Jean,
Nicolas Pierre
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)81104-4
Subject(s) - dermorphin , peptide , chemistry , opioid peptide , peptide sequence , frog skin , amino acid , oligopeptide , biochemistry , amphibian , opioid , microbiology and biotechnology , receptor , biology , gene , sodium , ecology , organic chemistry
The predicted amino acid sequence of the biosynthetic precursor of dermorphin, a highly potent and nearly specific μ‐opioid peptide from amphibian skin, contains four repeats of the dermorphin progenitor sequence and one single copy of a different heptapeptide sequence. We have developed a specific enzyme immunoassay and used synthetic peptides to detect and purify the new predicted heptapeptide 2.4 μg/g dry skin) from the skin of the Phyllomedusa sauvagei frog from which dermorphin was originally isolated. The identity of the novel pro‐dermorphin related peptide, Tyr‐D‐Met‐Phe‐His‐Leu‐Met‐Asp‐NH 2 , was established by co‐chromatography with synthetic peptides on reverse‐phase HPLC, immunological analysis, gas‐phase sequencing, mass spectrometry and by pharmacological assays. Opioid‐binding assays in vitro demonstrated that both the natural and synthetic heptapeptides displayed exceptionally high selectivity and affinity towards the δ‐opioid receptors. Because of its origin and its δ‐opioid (enkephalin) activity and specificity, this novel D‐amino acid containing peptide is named dermenkephalin.