Isolation of dermenkephalin from amphibian skin, a high‐affinity (δ‐selective opioid heptapeptide containing a D‐amino acid residue

  title={Isolation of dermenkephalin from amphibian skin, a high‐affinity ($\delta$‐selective opioid heptapeptide containing a D‐amino acid residue},
  author={Amram Mor and Antoine Delfour and Sandrine Sagan and Mohamed Amiche and Ph. Pradelles and Jean Rossier and Pierre Nicolas},
  journal={FEBS Letters},

Isolation, amino acid sequence, and synthesis of dermaseptin, a novel antimicrobial peptide of amphibian skin.

The synthetic replicate was shown to be indistinguishable from natural dermaseptin with respect to chromatographic properties, amino acid sequence determination, and mass spectrometry analysis.

Quantitative two‐dimensional nmr study of dermenkephalin, a highly potent and selective δ‐opioid peptide

The overall data should provide realistic starting models for energy minimization and modelization studies, and the nonuniform values of the temperature coefficient may reflect an equilibrium mixture of folded and extended conformers.

Characterization of D‐amino‐acid‐containing excitatory conotoxins and redefinition of the I‐conotoxin superfamily

Two related peptides are characterized, r11b and r11c, with d‐Phe and d‐Leu at the homologous position, with results indicate that neither the chemical nature of the side chain nor the precise vicinal sequence around the modified residue seem to be critical, but there may be favored loci for isomerization to a d‐amino acid.

Opioid activity of dermenkephalin analogues in the guinea‐pig myenteric plexus and the hamster vas deferens

The results obtained emphasise the importance of a negative charge at the C‐terminus of dermenkephalin for selectivity at the δ‐opioid receptor and the role that the d‐configuration plays in determining the bioactive folding of these highly active peptides.

Evidence for Pro-dermorphin processing products in rat tissues.

Opioid peptides from frog skin.

The similarity between the prepro-regions of precursors encoding end products with strikingly different structures and biological activities supports the suggestion that the genes encoding these peptides are all members of the same family.

A Novel cDNA Sequence Encoding the Precursor of the d‐Amino Acid‐Containing Neuropeptide Fulicin and Multiple α‐Amidated Neuropeptides from Achatina fulica

The results suggest that fulicin and related peptides are produced in neurons and the heart by the processing of a ribosomally made precursor, although the mechanism of in‐chain epimerization remains unclear.



Dermorphin and related peptides in rat tissues


1 Dermorphin and Hyp6‐dermorphin are the first representatives of a new class of potent opioid peptides occurring in amphibian skin. They present the unique feature of having a D‐Ala residue

Characterization of the receptor binding profile of (3H)-dermorphin in the rat brain.

The high affinity and selectivity of (3H)-dermorphin together with its very low nonspecific binding make this peptide a useful tool for dissecting the role of the mu-receptor(s) in inducing analgesia after intracerebroventricular administration.

Structural requirements for dermorphin opioid receptor binding.

While the whole dermorphin sequence is required for the expression of the full intrinsic binding activity of the molecule, the N-terminal tripeptide is a key structure as it contains the features which allow receptor recognition.

D-alanine in the frog skin peptide dermorphin is derived from L-alanine in the precursor.

A D-alanine-containing peptide termed dermorphin, with potent opiate-like activity, has been isolated from skin of the frog Phyllomedusa sauvagei and the existence of a novel post-translational reaction for the conversion of an L-amino acid to its D-isomer is suggested.

Amino acid composition and sequence of dermorphin, a novel opiate-like peptide from the skin of Phyllomedusa sauvagei.

Dermorphin presents striking differences from the known enkephalins; it offers a surprising example of a peptide from Vertebrata containing a D-amino acid residue in its sequence.

Synthesis and properties of dermorphin and an analog of beta-endorphin containing the dermorphin sequence.

Dermorphin (I) and [D-Ala2, Phe3, Gly4, Tyr5, Pro6]-beta c-EP (II) have been synthesized by the solid-phase method and represents a rare instance where the enkephalin moiety of beta-endorphin has been altered to produce a more potent analgesic.

An enzyme immunoassay for synthetic thymulin.