Dermorphin
Also known as: dermorphin peptide, DADL opioid
Dermorphin is a seven amino acid peptide that occurs naturally in the skin of South American frogs, including Phyllomedusa and related genera. It is studied in opioid pharmacology because it binds mu type opioid receptors with high affinity and selectivity.
Quick Reference
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Overview
Opioid agonist peptide compound
Dermorphin is a hepta-peptide first isolated from the skin of South American frogs belonging to the genus Phyllomedusa. The peptide is an agonist with high potency and selectivity to mu opioid receptors. Dermorphin is about 30–40 times more potent than morphine. The amino acid sequence of dermorphin is H-Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH2.
Mechanism of Action
Dermorphin acts mainly through mu type opioid receptors, for which it shows high affinity and selectivity in binding studies. Receptor activation by this peptide produces strong opiate like effects in experimental models, which is why researchers use it to probe mu receptor signaling.
Research History
Dermorphin was discovered in amphibian skin secretions, where frogs produce it as part of their chemical defenses. Its unusually strong and selective activity at mu opioid receptors made it a reference compound in opioid research, and related frog species were later found to produce their own versions of the peptide.
What Researchers Are Saying
Community Reports - Not Medical Advice
The following is aggregated from public forums, Reddit, and research communities. These are anecdotal reports from researchers only - not verified clinical data and not a recommendation of any kind.
Dermorphin (also known as dermorphin peptide, DADL opioid) is studied within the peptide research community. Heptapeptide opioid analogue from amphibian skin studied for potent analgesic activity.
Last updated October 28, 2026
Research status: limited. Dermorphin appears across peptide research forums and academic literature. Researchers note this compound falls in the other category.
Last updated October 28, 2026
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