Dermorphin 20mg

Description

Disclaimer: This compound is provided strictly for laboratory and scientific research purposes only. It is not approved by the U.S. Food and Drug Administration (FDA) for human or veterinary use, including ingestion, injection, or any form of administration.

Chemical Properties of Dermorphin

Property	Details
CAS Number	77614-16-5
Molar Mass	802.88 g/mol
PubChem CID	5485199
Chemical Formula	C40H50N8O10
IUPAC Name	(2S)-N-[(2S)-1-amino-3-hydroxy-1-oxopropan-2-yl]-1-[(2S)-2-[[2-[[(2S)-2-[[(2R)-2-[[(2S)-2-amino-3-(4-hydroxyphenyl)propanoyl]amino]propanoyl]amino]-3-phenylpropanoyl]amino]acetyl]amino]-3-(4-hydroxyphenyl)propanoyl]pyrrolidine-2-carboxamide
Stability/ Shelf life	Stable for up to 24 months when stored lyophilized under appropriate conditions
Synonyms	Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH₂; Dermorphin; DTXSID40228281
Purity	≥98%
Storage Instructions	Store lyophilized at −20°C, protected from light and moisture. Following reconstitution, store at 2–8°C and use within 30 days. Avoid repeated freeze-thaw cycles.
Solubility	Soluble in water and aqueous buffers
Peptide Class	Naturally derived heptapeptide; amphibian mu-opioid receptor agonist
Physical Form	Lyophilized white powder
DEA Status	Schedule I Controlled Substance (21 U.S.C. § 812). Research use in the United States requires appropriate DEA registration and compliance with applicable regulations
Wada Status	Prohibited in-competition under WADA Prohibited List S7 (Narcotics) as an opioid agonist class compound. Also prohibited in equine sport under ARCI Class I (Racing Commissioners International). Researchers in sport science or anti-doping contexts must verify current classification via GlobalDRO.com and applicable sport governing body regulations

Overview

Dermorphin is a naturally derived heptapeptide isolated from the skin of South American frogs of the genus Phyllomedusa. It is classified as a highly potent mu-opioid receptor (MOR)-selective peptide. In preclinical rodent antinociceptive assays, dermorphin demonstrates 30–40 times the analgesic potency of morphine, with greater than 1,000-fold selectivity for mu-opioid receptors over delta- and kappa-opioid receptor subtypes in radioligand binding studies. 

It is distinguished by the presence of a D-alanine residue at position 2. This is a rare example of naturally occurring post-translational D-amino acid incorporation in an animal-derived peptide. This structural feature confers enhanced enzymatic resistance relative to linear L-amino acid opioid peptides. [Amiche et al., 1998]

Dermorphin has not been approved by the FDA for human or veterinary use, including ingestion, injection, or any form of administration. It is not a dietary supplement or consumer product. Availability is restricted to qualified researchers at licensed institutions. Clinical research initiatives require guidance from the relevant Institutional Review Board (IRB). Preclinical animal studies must comply with IACUC directives under the Animal Welfare Act (AWA).

Note: In the United States, Dermorphin is classified as a Schedule I controlled substance under the  Controlled Substances Act (21 U.S.C. § 812).  Researchers must hold a valid DEA Schedule I  researcher registration before acquiring or handling this compound.

Working Mechanism of Dermorphin

Dermorphin has been investigated in preclinical models as a potent and selective mu-opioid receptor (MOR) agonist. Radioligand binding studies using tritiated dermorphin in rat brain membranes identified a single population of high-affinity binding sites with a Kd of 0.86 nM. Naloxone competitively inhibited specific binding with an IC₅₀ of 3.4 nM, confirming mu-opioid receptor mediation. [Amiche et al., 1987]

The mu-opioid selectivity of dermorphin has been attributed to its distinctive C-terminal region (Gly-Tyr-Pro-Ser-NH₂), which distinguishes it from the delta-selective deltorphin family despite sharing the same N-terminal Tyr-D-Xaa-Phe motif. All mechanistic findings are derived from in vitro and preclinical animal models only. Human pharmacology data are absent, and findings are not generalizable to human therapeutic outcomes. [Erspamer et al., 1989]

Research Findings / Research Applications

Preclinical investigations have examined Dermorphin in relation to:

Mu-Opioid Receptor Binding Characterization in Rat Brain Membrane Models

Based on articles retrieved from PubMed, high-affinity specific binding sites for Dermorphin were characterized in rat brain membrane preparations using tritiated dermorphin as the primary radioligand. Binding was saturable and time-dependent, with a Kd of 0.86 nM determined by Scatchard analysis. Dermorphin and naloxone displaced specific binding with IC₅₀ values of 1.6 nM and 3.4 nM, respectively, consistent with a single competitive binding site model. Findings are from in vitro rat brain membrane assays only and do not constitute clinical evidence.

[Amiche et al., 1987 — https://pubmed.ncbi.nlm.nih.gov/2825686/]

Antinociceptive Observations in Rodent Pain Models — Dermorphin Variant [Lys7]dermorphin

Based on articles retrieved from PubMed, the dermorphin variant [Lys7]dermorphin was examined for antinociceptive activity in rat and mouse models via multiple administration routes. Antinociceptive potency exceeding morphine by 290-fold intracerebroventricularly and 25–30-fold peripherally was reported. Mu-opioid receptor mediation was confirmed by naloxone and naloxonazine antagonism. Antinociceptive effects were also observed in a chronic inflammatory pain model using Freund’s adjuvant arthritis. Findings are from preclinical rodent experimental models only and have not been validated in human clinical settings.

[Negri et al., 1995 — https://pubmed.ncbi.nlm.nih.gov/7712029/]

Opioid Precursor Biology and D-Amino Acid Biosynthesis Research

Based on articles retrieved from PubMed, preprodermorphin precursors cloned from Phyllomedusa sauvagei and Phyllomedusa bicolor cDNA libraries were found to contain four to five homologous 35-amino acid repeats, each encoding a dermorphin progenitor sequence. The D-alanine at position 2 is encoded by a conventional L-alanine codon, indicating post-translational enzymatic isomerization. These findings have been examined in the context of gene-encoded opioid peptide biology and evolutionary relationships to amphibian antimicrobial peptide precursor families. Findings are from molecular biology and biochemical studies only.

[Amiche et al., 1998 — https://pubmed.ncbi.nlm.nih.gov/9949868/]

Important Note: These findings are derived from early-stage preclinical and in vitro research. Results are not consistent across all experimental models, and data remain limited without validation in human clinical settings.

Risks & Handling Information

Risk Tier: HIGH. Dermorphin is a potent mu-opioid receptor agonist with preclinical antinociceptive potency substantially exceeding morphine in rodent models. Its opioid receptor activity profile confers a high risk tier for laboratory handling. Any unintentional exposure should be treated as requiring immediate decontamination and medical consultation. 

PPE Requirement: Nitrile gloves, lab coat, and eye protection are required at all times. Additional respiratory protection is recommended during reconstitution and handling of the lyophilized powder, given the compound’s reported opioid receptor activity profile.

Controlled Environment: Handling must occur exclusively within controlled laboratory environments with adequate ventilation, appropriate containment, and institutional biosafety oversight. This compound must not be handled in non-laboratory settings under any circumstances.

Toxicological Status: The full toxicological profile of Dermorphin in human biological systems is not established. Researchers must adhere strictly to institutional biosafety protocols applicable to centrally active opioid-class research compounds.

Storage and Degradation Risk: Maintain lyophilized vials at −20°C until use. Following reconstitution, store at 2–8°C and use within 30 days. Avoid repeated freeze-thaw cycles and exposure to heat, light, or moisture to preserve research-grade peptide integrity.

FAQs

Q: What is the regulatory status of Dermorphin in the United States?

Dermorphin has not been approved by the FDA for human or veterinary use, including ingestion, injection, or any form of administration. It is available exclusively for qualified laboratory and scientific research purposes at licensed institutions operating under applicable institutional oversight frameworks.

Q: What is the structural basis for Dermorphin’s mu-opioid receptor selectivity?

Based on articles retrieved from PubMed, structure-activity studies have identified the C-terminal region Gly-Tyr-Pro-Ser-NH₂ as the primary determinant of dermorphin’s mu-opioid selectivity. The D-alanine at position 2 contributes to enzymatic resistance and receptor interaction profile. These structural features distinguish dermorphin from the delta-selective deltorphin family, sharing the same N-terminal Tyr-D-Xaa-Phe motif. [Erspamer et al., 1989]

Q: How does Dermorphin’s D-amino acid content arise biosynthetically?

Based on articles retrieved from PubMed, the D-alanine at position 2 is encoded by a conventional L-alanine codon in the preprodermorphin precursor mRNA. D-configuration arises post-translationally through an enzymatic isomerization process not yet fully characterized at the molecular level. [Amiche et al., 1998]

Q: Has Dermorphin been evaluated in human clinical research?

No peer-reviewed human clinical trials specific to Dermorphin have been published in indexed literature as of June 2026. Available research is derived from in vitro binding assays, isolated tissue pharmacology, and preclinical rodent models only.

Q: What storage conditions are required to maintain Dermorphin integrity for research use?

Lyophilized Dermorphin should be stored at −20°C, protected from light and moisture. Following reconstitution, store at 2–8°C and use within 30 days. Avoid repeated freeze-thaw cycles to preserve peptide integrity.

Q: What distinguishes Dermorphin from the deltorphin class of amphibian opioid peptides?

Based on articles retrieved from PubMed, both peptide families share the N-terminal Tyr-D-Xaa-Phe motif. Dermorphin’s C-terminal sequence Gly-Tyr-Pro-Ser-NH₂ confers mu-opioid selectivity, while the deltorphins carry anionic C-terminal residues (Asp or Glu) associated with delta-opioid receptor selectivity. These families are frequently studied together as complementary tool compounds in opioid receptor subtype pharmacology research. [Erspamer et al., 1989]

References

Amiche, M., Delfour, A., Morgat, J. L., Roy, J., Houvet, J., & Nicolas, P. (1987). Specific opioid binding sites for dermorphin in rat brain. Biochemical and Biophysical Research Communications, 148(3), 1432–1439. https://pubmed.ncbi.nlm.nih.gov/2825686/

Erspamer, V., Melchiorri, P., Falconieri-Erspamer, G., Negri, L., Corsi, R., Severini, C., Barra, D., Simmaco, M., & Kreil, G. (1989). Deltorphins: a family of naturally occurring peptides with high affinity and selectivity for delta opioid binding sites. Proceedings of the National Academy of Sciences USA, 86(13), 5188–5192. https://pubmed.ncbi.nlm.nih.gov/2544892/

Amiche, M., Delfour, A., & Nicolas, P. (1998). Opioid peptides from frog skin. EXS, 85, 57–71. https://pubmed.ncbi.nlm.nih.gov/9949868/

Negri, L., Lattanzi, R., & Melchiorri, P. (1995). Production of antinociception by peripheral administration of [Lys7]dermorphin. British Journal of Pharmacology, 114(1), 57–66. https://pubmed.ncbi.nlm.nih.gov/7712029/

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