Dermenkephalin is a seven-residue naturally occurring opioid peptide containing D-methionine at position 2. Its sequence, Tyr-D-Met-Phe-His-Leu-Met-Asp-NH₂, was identified from amphibian peptide precursors and displays unusually strong preference for the δ-opioid receptor.

Product Information

A Natural Peptide Containing a D-Amino Acid

Dermenkephalin belongs to the unusual group of animal peptides biosynthesized with a D-amino-acid residue. D-Met2 is important for its receptor-active conformation and contributes to resistance against conventional peptide degradation pathways.

Message and Address Domains

Structure–activity studies separated the molecule into an N-terminal opioid “message” region and a C-terminal δ-receptor “address” region.

His4-Leu5-Met6-Asp7-NH₂ strongly contributes to directing the ligand toward δ receptors, while Asp7 helps reduce recognition at μ-opioid sites. This provides a classic experimental model for receptor-selective peptide design.

High δ-Receptor Selectivity

Historical receptor studies characterized Dermenkephalin as a highly potent δ-opioid agonist with much lower affinity for μ-opioid receptors.

We recommend using receptor-specific experimental controls rather than treating published selectivity ratios as universal constants across species or assay platforms.

Analytical Considerations

Two methionine residues are present at positions 2 and 6. Oxidation state is therefore especially relevant during storage and LC-MS analysis.

Frequently Asked Questions

What makes Dermenkephalin unusual?

It contains naturally occurring D-Met at position 2 and has pronounced δ-opioid receptor selectivity.

Which region contributes to δ selectivity?

The C-terminal His-Leu-Met-Asp-NH₂ region functions as an important δ-receptor address domain.

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