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Opioid peptides from frog skin

M Amiche1, A Delfour, P Nicolas

  • 1Laboratoire de Bioactivation des Peptides, Institut Jacques Monod, Paris, France.

EXS
|February 9, 1999
PubMed
Summary

South American frogs secrete unique opioid peptides with D-amino acids, like dermorphin and deltorphins, which are highly selective for opioid receptors. These peptides and antimicrobial peptides share common gene precursors, suggesting a shared evolutionary origin.

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Area of Science:

  • Biochemistry
  • Pharmacology
  • Evolutionary Biology

Background:

  • South American Phyllomedusa frogs' skin secretions contain novel gene-encoded opioid peptides.
  • These peptides feature a D-amino acid at position 2, a characteristic not typical in mammalian peptides.
  • Examples include dermorphin, dermenkephalin/deltorphin A, and deltorphins, known for high potency and selectivity at mu- and delta-opioid receptors.

Purpose of the Study:

  • To investigate the nature and origin of D-amino acid-containing opioid peptides in frog skin.
  • To explore the genetic relationship between opioid peptides and antimicrobial peptides found in amphibian precursors.
  • To understand the evolutionary implications of shared gene families encoding diverse peptide functions.

Main Methods:

  • Peptide sequencing and characterization of skin secretions.
  • Analysis of messenger RNA (mRNA) to confirm D-amino acid coding.
  • Comparative sequence analysis of precursor proteins for opioid and antimicrobial peptides.

Main Results:

  • Identification of dermorphin, dermenkephalin/deltorphin A, and deltorphins with D-amino acids (D-Ala, D-Met).
  • Confirmation that D-amino acids are encoded by standard codons in the respective mRNAs.
  • Significant sequence similarities found between prepro-regions of precursors for opioid peptides and antimicrobial peptides (dermaseptins, brevinins, etc.).

Conclusions:

  • The D-amino acid-containing opioid peptides from Phyllomedusa frogs are potent and selective opioid receptor ligands.
  • The genetic data suggest that genes encoding these diverse peptides belong to the same evolutionary family.
  • This finding highlights a shared evolutionary pathway for peptides with distinct structures and biological activities in amphibians.

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