Dermorphin
Amphibian-derived opioid peptide
A potent amphibian mu-opioid peptide — strictly research-only.
Half-life
~ short to moderate (D-amino acid extends stability)
Mol. weight
802.9 g/mol
Sequence
Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser
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Overview
Dermorphin is a heptapeptide originally isolated from the skin of South American frogs. It is a potent and selective mu-opioid receptor agonist — substantially more potent than morphine in animal models — and is included in the library strictly for pharmacological education, not therapeutic use.
Mechanism of action
Dermorphin binds the mu-opioid receptor with high affinity, producing analgesia in animal models far more potently than morphine. Its D-amino acid (D-Ala) residue confers partial resistance to enzymatic degradation. As an opioid-class compound, it carries the full risk profile of opioid pharmacology including respiratory depression and dependence liability.
Researched benefits
- Potent analgesic activity in preclinical models
- Useful pharmacological tool for opioid receptor research
- D-amino acid structure studied for stability
Considerations
- Opioid-class compound with dependence and respiratory-depression liability
- Scheduled/restricted in many jurisdictions
- Included for educational purposes only — not for use
- Not FDA-approved
Key Academic Literature & Studies
Search more in PubMedPeer-reviewed citations and clinical trials evaluating Dermorphin in scientific literature.
Query PubMed for recent peer-reviewed preclinical and clinical publications on Dermorphin:
View Dermorphin index on PubMed (NCBI)