Dermorphin
From CAD $50 CAD $56
Size: 5mg
Contents: Dermorphin (Opioid Heptapeptide Agonist)
Form: Powder
Purity: 99.3%
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- PURITY
- STERILITY
- WEIGHT
- ENDOTOXINS(LPS)

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Dermorphin Peptide
Dermorphin is a naturally occurring heptapeptide belonging to the class of endogenous opioid-like peptides. It was originally isolated from the skin secretions of Phyllomedusa tree frogs. Dermorphin exhibits high selectivity and affinity for the μ-opioid receptor (MOR) and has been studied in research settings for its unique receptor-binding properties, potent analgesic activity, and neurophysiological effects. This compound is supplied exclusively for research and analytical use.
Overview
Dermorphin acts primarily as a potent and selective agonist of the μ-opioid receptor. Its amino acid sequence (H-Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH₂) contains a D-alanine residue in the second position—an uncommon feature in mammalian peptides—which is believed to contribute to its high receptor affinity and resistance to enzymatic degradation.
In experimental models, Dermorphin has demonstrated significantly greater binding potency at the μ-opioid receptor compared to endogenous ligands such as β-endorphin and morphine. It has been used in receptor pharmacology studies to explore opioid receptor signaling, pain modulation, and G-protein–coupled receptor (GPCR) dynamics.
Research also suggests possible applications in neurobiology and behavioral science due to Dermorphin’s influence on synaptic transmission, nociception, and neuronal excitability.
Chemical Makeup
- Molecular Formula: C₄₀H₅₀N₈O₁₀
- Molecular Weight: 802.88 Da
- Observed Mass (Batch # 2025034): 802.9 Da
- Purity (HPLC, LCMS-confirmed): 99.09 %
- Form: Lyophilized powder
- Analysis Method: Reverse-phase HPLC (UV 214 nm) and LCMS (ESI+ mode), calibrated with synthetic Dermorphin reference standard.
- Appearance: White to off-white powder
Research and Preclinical Studies
μ-Opioid Receptor Binding and Selectivity
Dermorphin has been shown to possess high selectivity for μ-opioid receptors over κ- and δ-opioid subtypes. Radioligand binding assays have confirmed strong MOR affinity and slow dissociation kinetics, making it valuable in receptor-binding characterization and signal transduction studies.
Analgesic Mechanisms
In preclinical research, Dermorphin has been used as a model compound for examining endogenous opioid pathways and pain regulation. Experimental data indicate that it can produce prolonged analgesic responses compared to morphine when administered in controlled systems, allowing for comparative opioid receptor activity studies.
Neurochemical and Behavioral Studies
Research involving Dermorphin has investigated its influence on neurotransmitter release, nociceptive signaling, and neuronal firing patterns. These studies aim to better understand GPCR modulation, receptor desensitization, and neuroadaptive responses associated with opioid receptor activation.
Summary
Dermorphin (Batch # 2025034) exhibits an LCMS-confirmed molecular mass of 802.9 Da and a measured purity of 99.09 %. Analytical verification confirms its suitability for advanced laboratory investigations involving receptor pharmacology, neurochemical signaling, and pain modulation research. This compound is strictly for research use only.
References
- Montecucchi PC, De Castiglione R, Piani S, Gozzini L, Erspamer V. “A novel amphibian skin peptide with potent opiate-like activity.” Nature. 1981;292(5826):608-610. https://pubmed.ncbi.nlm.nih.gov/7198101/
- Erspamer V, et al. “Dermorphin: a potent natural analgesic peptide from amphibian skin.” Eur J Pharmacol. 1982;78(3):337-342. https://pubmed.ncbi.nlm.nih.gov/6288442/
- Negri L, et al. “Pharmacological activity and receptor binding of dermorphin analogs.” Peptides. 1985;6(Suppl 3):87-91. https://pubmed.ncbi.nlm.nih.gov/2413894/
- Broccardo M, et al. “Central and peripheral activity of dermorphin in animal models.” Br J Pharmacol. 1981;73(3):625-631. https://pubmed.ncbi.nlm.nih.gov/6264952/
- Li CH, Chung D. “Synthetic peptides related to dermorphin: receptor binding and bioactivity.” Biochemistry. 1983;22(8):1923-1928. https://pubmed.ncbi.nlm.nih.gov/6300120/
- Lazzeri G, Negri L, et al. “Receptor selectivity of dermorphin analogues.” Eur J Pharmacol. 1985;110(3):357-363. https://pubmed.ncbi.nlm.nih.gov/2988703/
- Stefano GB, et al. “Opiate receptor activity in invertebrate and vertebrate systems: insights from dermorphin analogues.” Proc Natl Acad Sci USA. 1989;86(22):8977-8981. https://pubmed.ncbi.nlm.nih.gov/2573076/
- Williams JT, Christie MJ, Manzoni O. “Cellular and synaptic adaptations mediating opioid dependence.” Physiol Rev. 2001;81(1):299-343. https://pubmed.ncbi.nlm.nih.gov/11152759/
- DrugBank Online. “Dermorphin.” https://go.drugbank.com/drugs/DB13355
- National Center for Biotechnology Information. “Dermorphin compound summary.” https://pubchem.ncbi.nlm.nih.gov/compound/Dermorphin
For research use only. Not for human or veterinary use.

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Every vial we sell comes from a lab that follows current Good Manufacturing Practices (cGMP). That means each step of production is documented and controlled. Before a batch is released, it’s tested by independent third-party labs for purity, identity, and sterility. Certificates of analysis are available so you can see the exact test results.
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Peptides in lyophilized (freeze-dried) form are stable at room temperature for transport. Once you receive them, refrigeration is recommended to maintain long-term integrity. We package every order securely to prevent damage and ship promptly, so your vials arrive in optimal condition.
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We operate under strict in-house protocols that follow current Good Manufacturing Practices (cGMP). That means our team oversees the entire process from sourcing raw amino acids to the final lyophilized vial. Nothing is outsourced or repackaged. This gives us full control over purity, consistency, and sterility, and it’s why we can stand behind every single vial we ship.
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