Description
Dermorphin is an opioid heptapeptide (Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser) originally isolated from the skin of South American Phyllomedusa frogs. The unusual D-alanine amino acid at position 2 makes the peptide resistant to enzymatic degradation and dramatically increases binding affinity at the Mu opioid receptor.
Per study reports Dermorphin binds selectively at the Mu opioid receptor with about 30-40x higher potency than morphine per mole. Analgesic action is correspondingly strong, with lower respiratory depression relative to analgesic action compared to classical opiates.
Dermorphin has a controversial history in horse racing - it was discovered in the 2010s as illegal doping compound in several horse racing scandals, with action as performance enhancer through pain masking.
In human recreational research Dermorphin is practically unestablished. The substance remains primarily a preclinical compound of opioid receptor pharmacology. Like all Mu opioid agonists, dependence potential exists.
You can order Dermorphin as lyophilized peptide in 10-pack at 5mg per vial.
This information is for research and educational purposes only. No medical recommendations.
Risks & Safety
Dermorphin is an opioid heptapeptide with high Mu receptor selectivity and a potency documented in the literature well above that of morphine. The compound therefore carries the full risk profile of the opioid class and is considerably higher-risk than most peptides.
Documented in the literature and opioid pharmacology:
- Respiratory depression: like all Mu opioid agonists, dermorphin can depress respiration at higher dosages. The high potency per mole makes dosing errors particularly consequential.
- Dependence potential: Mu opioid agonists have a documented tolerance and dependence potential with repeated exposure.
- Sedation: sedation, drowsiness and reduced alertness are classical opioid effects and are described in the literature.
- Dangerous combinations: with other opioid agonists or benzodiazepines, additive to synergistic respiratory depression is documented.
- No human data: dermorphin is practically unestablished in human use; no robust safety studies exist outside the preclinical context.
This classification does not replace medical advice. Risk and responsibility for any actual use lie entirely with the buyer.
Studies
- Amino acid composition and sequence of dermorphin, a novel opiate-like peptide from the skin of Phyllomedusa sauvagei - International Journal of Peptide and Protein Research 1981, Montecucchi et al: original sequence identification of the heptapeptide.
- Dermorphin: Central sites of analgesia, catalepsy, and inhibition of gastric secretion and emptying, in rats - Regulatory Peptides 1983, Melchiorri et al: central nervous system action characterization.
- Cross-tolerance between dermorphin and morphine to analgesia and catalepsy in rats - Peptides 1985, Broccardo et al: Mu-opioid pharmacology study on tolerance relationship.
- Dermorphin-related peptides from the skin of Phyllomedusa bicolor and their amidated analogs activate two mu opioid receptor subtypes that modulate antinociception and catalepsy in the rat - PNAS 1992, Negri et al: Mu receptor subtype characterization.
- Detection, quantification, and identification of dermorphin in equine plasma and urine by LC-MS/MS for doping control - Analytical and Bioanalytical Chemistry 2013, Guan et al: horse racing detection methodology.
