Dermorphin is an extremely potent compound that can cause serious harm or death if handled or used improperly. There is very limited research on its safety, and it should only be used in controlled laboratory settings by qualified professionals.
- OP Labs formerly Oxford Peptides.
- Batch HPLC tested at 99%+ purity.
- Store frozen long term or in fridge when ready to be used.
- Sold for research purposes only.
- Contact us for Wholesale Orders.
Download COA here: Dermorphin_COA.pdf
Please note: if you have a different Batch ID please contact us for the latest COA.
Dermorphin
Dermorphin is a naturally occurring heptapeptide originally isolated from the skin secretions of South American frogs of the genus Phyllomedusa. It is classified as a non-mammalian opioid peptide and is not endogenously produced in humans or other mammals.
Dermorphin exhibits high affinity and selectivity for the μ-opioid receptor (MOR) and is notable for the presence of a D-amino acid (D-alanine) within its sequence, a feature that arises from post-translational amino acid epimerization rather than direct ribosomal synthesis. This uncommon biochemical modification distinguishes dermorphin from typical mammalian opioid peptides and makes it a subject of interest in peptide chemistry and receptor–ligand interaction research.
In biochemical and pharmacological research systems, dermorphin is used as a reference compound for studying μ-opioid receptor binding, signal transduction, and structure–activity relationships of opioid peptides. Experimental observations are dependent on model system, concentration, and assay design, and are used for mechanistic investigation rather than defined biological or clinical outcomes.
Synonyms: Dermorphin peptide; Frog skin opioid peptide
Peptide Length: 7 amino acids
Peptide Classification: Naturally occurring heptapeptide; μ-opioid receptor agonist
CAS Number: 65107-26-6
Molecular Formula: C40H50N8O10
Molecular Weight: ~802.9 g/mol
Appearance: White to off-white lyophilised powder
Purity: ≥ 99% (HPLC, typical)
Solubility: Soluble in water and buffered aqueous solutions
Storage: –20 °C, desiccated, protected from light
Pack Size: 10 mg
Applications in Research
• μ-opioid receptor binding and signalling studies
• Structure–activity relationship (SAR) investigations of opioid peptides
• Comparative studies of D-amino acid–containing peptides
• Reference compound for non-mammalian opioid systems
Handling & Stability
• Handle only by trained personnel using appropriate laboratory controls
• Reconstitute in sterile water or suitable buffered solution
• Avoid repeated freeze–thaw cycles
• Prepare working solutions fresh where possible
• Protect from light, moisture, and extreme pH
Specifications Summary
Purity: ≥ 99% (HPLC)
Appearance: White to off-white lyophilised powder
Peptide Type: Natural heptapeptide (frog-derived)
Molecular Weight: ~802.9 g/mol
Solubility: Water, buffered aqueous solutions
Storage: –20 °C, desiccated, dark
Precautions & Notes
• Dermorphin is highly potent and requires strict laboratory handling procedures
• Experimental behaviour depends on receptor expression and assay conditions
• Not intended for therapeutic, diagnostic, or cosmetic use
• For laboratory research use only
References
Melchiorri P., Negri L. The dermorphin peptide family. General Pharmacology, 1996.
https://pubmed.ncbi.nlm.nih.gov/8981054/
Amiche M. et al. Opioid peptides from frog skin. D-Amino Acids in Secreted Peptides, 1998.
https://pubmed.ncbi.nlm.nih.gov/9949868/
Broccardo M. et al. Pharmacological data on dermorphins. British Journal of Pharmacology, 1981.
https://pubmed.ncbi.nlm.nih.gov/7195758/
Kreil G. Peptides containing a D-amino acid from frogs and molluscs. Journal of Biological Chemistry, 1994.
https://pubmed.ncbi.nlm.nih.gov/8157620/
Heck S.D. et al. Posttranslational amino acid epimerization in peptide chains. Proceedings of the National Academy of Sciences, 1996.
https://pmc.ncbi.nlm.nih.gov/articles/PMC39482/
Keywords: Dermorphin, opioid peptide, μ-opioid receptor agonist, frog skin peptide, D-amino acid peptide










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