Also known as: Frog Opioid Peptide, YAGFLM-NH2
Half-life: ~30-60 minutes
Last reviewed: · Published:
Dermorphin is a seven-amino-acid peptide originally isolated from the skin of South American Phyllomedusa frogs (most notably Phyllomedusa sauvagei). It is one of the most potent endogenous opioid receptor agonists known, with selective activity at the μ-opioid receptor (MOR) and analgesic potency in animal models 30-40 times greater than morphine on a per-mole basis. The peptide contains an unusual D-alanine at position 2 — one of the few naturally occurring D-amino acids found in vertebrates — which is essential for its potency and stability against enzymatic degradation.
Dermorphin has been of substantial pharmacological research interest since its discovery, as a probe for μ-opioid receptor pharmacology and as a starting point for the design of synthetic opioid analgesics. It has also gained notoriety as a doping agent in horse racing, where it has been detected in multiple high-profile cases of horses found to have anomalous analgesia or performance enhancement. Several US racing jurisdictions have specific regulations against Dermorphin use.
This peptide is included on this site for completeness because it is sold by uk-peptides.com and other research-chemical vendors. It is not a wellness peptide. Dermorphin is a potent opioid with all the addiction, respiratory-depression, and overdose risks of other strong opioids — those risks are likely amplified rather than reduced by the higher receptor selectivity and potency. Use of Dermorphin outside of a properly designed and reviewed research protocol is unsafe, very likely illegal (as an unscheduled opioid in most jurisdictions), and almost always inappropriate.
Dermorphin was first isolated and characterized in 1980 by the Italian research group of Pietro Melchiorri and Vittorio Erspamer from the skin secretions of Phyllomedusa sauvagei. Erspamer's prior work had established the existence of biologically active peptides in amphibian skin (he had previously discovered bombesin and other peptides). The unusual D-amino acid content and high μ-opioid receptor selectivity of dermorphin opened new directions in opioid pharmacology. The peptide has remained a research tool and a recognized doping agent in equine sport, but has never been developed for legitimate human clinical use.
Dermorphin is acutely tolerated as expected for a potent opioid — that is to say, it produces all the effects and risks of an opioid drug. Repeated use produces tolerance, physical dependence, and the full constellation of opioid use disorder risks. Overdose is a meaningful risk because of the high per-mole potency: errors in dosing are amplified relative to morphine. This is not a peptide suitable for self-experimentation or off-protocol use under any circumstances.
Dose Range
Per protocol (typically µg/kg)
Frequency
Per protocol
Duration
Per protocol
Dose Range
Not appropriate under any circumstances
Frequency
—
Duration
—
Dosing information is for educational purposes only. Consult a healthcare professional before using any peptide.
Typical Vial Size
2 mg
Water Type
Bacteriostatic water (BAC water)
Mixing Volume
1-2 mL
Half-Life
~30-60 minutes
Molecular Weight
802.9 Da
Store reconstituted vial refrigerated at 2-8°C. Use within 14-21 days. Note: this is a research opioid with all the risks of high-potency opioid drugs. Self-administration carries serious risk of overdose and addiction.
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FDA Status
Not FDA approved. Not scheduled in the US (research peptide status), but functionally an unregulated opioid.
Legal Status
Legal status varies by jurisdiction. Banned in equestrian sport. Recognized as a doping agent. Sale and use as a research chemical exists in a regulatory grey zone in most countries.
USA
Not approvedResearch chemical; banned by major racing jurisdictions
EU
Not approvedNot authorized as medicinal product; banned in equestrian sport
UK
Not approvedClassified as research chemical; equestrian sport banned
Australia
Not approvedTGA has not authorized; equestrian sport banned
Canada
Not approvedNot authorized for human use
Erspamer V, Melchiorri P, Falconieri-Erspamer G, Negri L, Corsi R, Severini C, Barra D, Simmaco M, Kreil G
Proceedings of the National Academy of Sciences (1989)
Comprehensive overview of the amphibian opioid peptide family discovered by the Erspamer group, including dermorphin and the related deltorphins, establishing the unusual D-amino acid pharmacology that defines this peptide class.
View Study →Broccardo M, Erspamer V, Falconieri Erspamer G, Improta G, Linari G, Melchiorri P, Montecucchi PC
British Journal of Pharmacology (1981)
Original pharmacological characterization of dermorphin demonstrating its potent CNS opioid activity and establishing its position as one of the most potent natural μ-opioid agonists known.
View Study →Maylin GA, Carlson G
Journal of Analytical Toxicology (2013)
Forensic / regulatory analysis of dermorphin detection in racing horse samples, illustrating the doping context that drives much of the modern regulatory and analytical interest in this peptide.
View Study →Track Dermorphin and more with PinnyPeptide.
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