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Dermorphin (Amphibian μ-Opioid Heptapeptide)

Research and Regulatory Scientific Reference | PubChem CID 5485199 H-Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH₂ | C₄₀H₅₀N₈O₁₀ | MW 802.88 g/mol μ-Opioid Receptor Agonist | D-Amino Acid-Containing Amphibian Heptapeptide | Phyllomedusa-Derived NOT FDA-Approved | Research Use Only | Class I Banned Substance (ARCI) | CAS 77614-16-5

REGULATORY STATUS — READ BEFORE PROCEEDING Dermorphin (CAS 77614-16-5; PubChem CID 5485199) is a naturally occurring opioid heptapeptide first isolated from the skin secretions of South American frogs of the genus Phyllomedusa. It is NOT approved by the U.S. Food and Drug Administration (FDA) for any human or veterinary indication. No IND, NDA, or ANDA exists for dermorphin in the United States.
Dermorphin has never entered human clinical trials. Its regulatory footprint in the United States derives entirely from enforcement action: FDA Office of Criminal Investigations and DOJ prosecutions arising from the 2011–2013 equine-doping scandals, and ongoing classification as a Class I banned substance by the Association of Racing Commissioners International (ARCI) — the most restrictive category, reserved for compounds with no accepted therapeutic use in horses and high abuse potential.
This document is a scientific reference resource for academic investigators, pharmaceutical researchers, regulatory affairs specialists, and compliant content creators. It is not a product listing, not a dosing guide, not a clinical protocol, and does not constitute any recommendation for human or veterinary use. Dermorphin must not be framed as a gray-market analgesic, performance enhancer, or research-chemical for personal use.
FDA confirmed in DOJ press materials (2018) that dermorphin is not approved for human or animal use and that its illicit distribution constituted illegal drug distribution and misbranding. Any U.S.-facing peptide business treating dermorphin as a consumer product faces serious regulatory and legal risk.

Product overview

Dermorphin is a naturally occurring opioid heptapeptide first isolated in 1981 from the skin secretions of the South American frog Phyllomedusa sauvagei by Erspamer, Melchiorri, and colleagues. Its canonical seven-residue sequence — H-Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH₂ — encodes a structural feature that is highly unusual in vertebrate biology but central to its pharmacology: a D-alanine residue at position 2. This single D-amino acid substitution protects the N-terminal Tyr-Ala bond from rapid enzymatic cleavage by aminopeptidases and dipeptidyl peptidase-4 (DPP-4), which would otherwise inactivate the opioid pharmacophore in plasma and tissues within seconds.

The net result is that dermorphin retains its receptor-active form in circulation far longer than endogenous opioid peptides such as enkephalins or endorphins, and the D-Ala2 modification simultaneously optimizes the geometry of the Tyr-D-Ala pharmacophore for high-affinity binding to the μ-opioid receptor (MOR). Experimental pharmacology data in standard rodent analgesia models place dermorphin at approximately 30–40 times more potent than morphine after systemic administration and up to 3,000–5,000 times more potent after intrathecal (spinal) injection.

Dermorphin belongs to the broader family of amphibian opioid skin peptides that includes deltorphins (selective δ-opioid receptor agonists) and other Phyllomedusa-derived compounds. Together these peptides have provided pharmacologists with important tools for dissecting opioid receptor subtypes, designing selective probes, and understanding the molecular basis of opioid analgesia, tolerance, and dependence. However, despite its extraordinary pharmacological potency, dermorphin has never progressed to human clinical development: no IND application, NDA, or formal clinical trial record exists in the United States.

Dermorphin’s public profile in the U.S. is dominated by enforcement history. Between 2011 and 2013, synthetic dermorphin was illegally administered to racehorses by a criminal network that exploited its analgesic and stimulant-like effects to mask pain and enhance performance. Federal prosecutions, FDA Office of Criminal Investigations involvement, and permanent Class I classification by the Association of Racing Commissioners International (ARCI) followed. For the 2026 U.S. peptide market, dermorphin is therefore squarely in YMYL and enforcement-sensitive territory: any content covering dermorphin must remain strictly educational, heavily cited, and unambiguous about non-approval and doping history.

DERMORPHIN CHEMICAL IDENTITY — REGISTRY AND STRUCTURAL REFERENCE

PubChem CID 5485199 — Authoritative Identity Anchor

PubChem CID 5485199 is the primary compound-level registry record for the dermorphin base peptide (C₄₀H₅₀N₈O₁₀, MW ≈802.88 g/mol, CAS 77614-16-5), maintained by the National Library of Medicine. This record consolidates structural data, SMILES identifiers, synonyms, pharmacological annotations, and links to related records. For salt forms used in research applications, PubChem CID 163335308 records dermorphin acetate, which includes the acetate counter-ion in its formula and yields a slightly higher molecular weight. Both CIDs provide 2D structure diagrams suitable for educational embedding.

THE D-AMINO ACID DESIGN — WHY DERMORPHIN IS PHARMACOLOGICALLY EXCEPTIONAL

Structural Basis of Potency and Selectivity

Mammalian endogenous opioid peptides — enkephalins, endorphins, dynorphins — all contain exclusively L-amino acids and are rapidly degraded in vivo by aminopeptidases, endopeptidases, and DPP-4. Their plasma half-lives are measured in minutes or seconds. Dermorphin’s extraordinary potency and duration relative to endogenous opioids stem primarily from two structural features that act in concert: the D-alanine at position 2 (D-Ala2) and the C-terminal primary amide.

The combined effect is a heptapeptide that binds the mu-opioid receptor with very high affinity while resisting the enzymatic machinery that rapidly clears endogenous opioid peptides. In guinea pig ileum (GPI) bioassays, dermorphin potently inhibits electrically evoked contractions — a functional hallmark of mu-agonist activity. In mouse vas deferens (MVD) preparations, which are more sensitive to delta-opioid agonists, dermorphin is substantially less active,confirming its selectivity profile. All pharmacological effects are fully reversed by naloxone, the archetypal opioid antagonist.

MECHANISM OF ACTION AND PHARMACOLOGY

μ-Opioid Receptor Agonism — Molecular and Systems Pharmacology

Dermorphin acts as a selective mu-opioid receptor (MOR) agonist. The MOR (OPRM1 gene product) is a class A G-protein-coupled receptor (GPCR) expressed in the central nervous system (brainstem, spinal cord, limbic system), peripheral nervous system, and gastrointestinal tract. MOR activation by dermorphin initiates Gi/Go-mediated signaling: adenylyl cyclase inhibition, cAMP reduction, activation of inwardly rectifying potassium channels (GIRK), inhibition of voltage-gated calcium channels, and downstream modulation of neuronal excitability and transmitter release. These cellular actions translate into the systemic opioid pharmacology observed in rodent research models: supraspinal and spinal analgesia, sedation, respiratory depression at high doses, gastrointestinal motility reduction, and dose-dependent euphoria.

Structure–Activity Relationships and Comparative Potency

The structure–activity relationships (SAR) of dermorphin and its synthetic analogs have been studied extensively since the 1980s as tools for dissecting mu-receptor pharmacology. Key SAR findings from peer-reviewed literature:

• D-Ala2 is non-negotiable for potency: replacing D-Ala2 with L-Ala2 causes a dramatic loss of mu-receptor affinity and functional potency, confirming that the D-configuration is the primary structural driver of dermorphin’s pharmacology.
• Tyr1 is the anchor residue: the N-terminal tyrosine hydroxyl group and aromatic ring are essential for all opioid receptor interactions, consistent with the classical opioid pharmacophore model (Tyr-Gly-Gly-Phe or equivalent).
• C-terminal amide vs free acid: amidation of Ser7 enhances receptor affinity and metabolic stability; the free-acid form is less active.
• Position 7 modifications (Lys7-NH2, Trp4/Asn7 substitution) shift the balance between antinociceptive and cataleptic effects, suggesting that C-terminal residues engage receptor subtypes or signaling conformations differently.
• Analogs retaining D-Ala2 and Tyr1 but with varied C-terminal sequences have been used as pharmacological probes for mu-receptor subtype characterization and receptor-ligand microenvironment mapping.
• Deltorphins (also from Phyllomedusa skin) contain D-Met or D-Ala at position 2 but have different address sequences (Asp4/Glu4 vs Gly4 in dermorphin) that confer high delta vs mu selectivity, illustrating how subtle C-terminal sequence changes redirect receptor targeting.

SAFETY PROFILE — MU-OPIOID CLASS EFFECTS AND HIGH-RISK DESIGNATION

IMPORTANT SAFETY CONTEXT Dermorphin has never undergone human clinical safety evaluation. The safety profile summarized below is derived from animal research models and from the class-effect profile of mu-opioid receptor agonists. There is NO established therapeutic index, NO safe human dose, and NO clinical guidance for dermorphin in humans or animals. This section is provided for scientific reference only.

EQUINE DOPING HISTORY — FROM FROG SKIN TO FEDERAL PROSECUTION (2011–2026)

Legal analysts and racing-industry commentators describe the 2011–2013 dermorphin doping cases as among the most significant equine drug-cheating scandals in American racing history, both for the novelty of the compound involved and the scope of the federal enforcement response.

U.S. REGULATORY FRAMEWORK — DERMORPHIN (2026)

U.S. PEPTIDE MARKET CONTEXT AND COMPETITIVE ENVIRONMENT (2026)

Understanding dermorphin’s position within the broader 2026 U.S. research-peptide landscape requires distinguishing it from the large class of non-approved but commercially active research peptides (BPC-157, TB-500, GHK-Cu, Epithalon, and similar), and from FDA-approved drugs with opioid activity. Dermorphin sits in a uniquely high-risk position:

1. Unlike BPC-157, TB-500, or GHK-Cu, dermorphin is not a gray-market peptide with an ambiguous FDA status — it has an active enforcement record from federal criminal prosecutions and is a banned Class I substance in regulated equine sports.
2. Unlike FDA-approved opioids (morphine, oxycodone, buprenorphine), dermorphin has no approved indication, no prescribing pathway, and no legitimate medical supply chain.
3. The 2026 U.S. research-peptide market has come under increased FDA and FTC scrutiny following the GLP-1 compounding enforcement wave. Enforcement attention is highest for compounds with (a) opioid-class pharmacology, (b) doping history, and (c) no approved indication. Dermorphin meets all three criteria.
4. Any U.S.-facing website covering dermorphin in non-educational, protocol-adjacent, or consumer-directed framing faces a high probability of FDA warning letters, FTC action, payment processor deplatforming, and Google content quality penalties under YMYL/E-E-A-T standards.
5. Legitimate commercial interest in dermorphin is confined to academic research institutions, pharmaceutical companies developing novel mu-opioid probes or pain therapeutics, and forensic/analytical laboratories developing doping-control methods.

FREQUENTLY ASKED QUESTIONS — SCIENTIFIC AND REGULATORY REFERENCE

Q1: What is dermorphin’s PubChem identifier, molecular formula, and CAS number?

Dermorphin’s primary PubChem record is Compound ID (CID) 5485199, with molecular formula C₄₀H₅₀N₈O₁₀, molecular weight approximately 802.88 g/mol, and CAS number 77614-16-5. The dermorphin acetate salt is recorded at PubChem CID 163335308. The authoritative compound record at https://pubchem.ncbi.nlm.nih.gov/compound/5485199 provides 2D structure diagrams, canonical SMILES, InChI identifiers, synonyms, and cross-links to pharmacological databases. These records are the appropriate identity anchors for any research or educational content.

Q2: Why is dermorphin so much more potent than morphine?

Two structural features drive dermorphin’s exceptional potency relative to morphine. First, the D-alanine residue at position 2 (D-Ala2) blocks aminopeptidase and DPP-4-mediated degradation at the Tyr1-D-Ala2 N-terminal bond, preserving the active pharmacophore in biological fluids far longer than endogenous L-amino acid opioid peptides. Second, the D-Ala2 substitution optimizes the spatial geometry of the Tyr1-D-Ala2 opioid pharmacophore for high-affinity mu-opioid receptor engagement. The C-terminal primary amide (Ser7-NH₂) contributes additional metabolic stability and receptor affinity. The net effect is extraordinary potency: approximately 30–40× greater than morphine systemically and up to 3,000–5,000× greater intrathecally in rodent models.

Q3: What is dermorphin’s FDA approval status in 2026?

Dermorphin is not approved by the FDA for any human or veterinary indication as of June 2026. No NDA, IND, or ANDA exists. The FDA confirmed in federal court proceedings in 2018 that dermorphin is not approved for human or animal use. There is no recognized 503A or 503B human compounding pathway for dermorphin. The only lawful U.S. positioning for dermorphin in 2026 is as a research-use-only (RUO) compound for legitimate academic or pharmaceutical research, labeled explicitly for in vitro or animal use only.

Q4: What were the dermorphin equine doping cases?

Between 2011 and 2013, synthetic dermorphin was illegally administered to racehorses across multiple U.S. states. Court records from federal proceedings in 2018 (DOJ/FDA-OCI) describe a criminal network in which a compounding pharmacy procured synthetic dermorphin from a chemical supplier, repackaged it under the coded name ‘D-Peptide,’ and distributed it to veterinarians who loaded pre-filled syringes for trainers to administer shortly before races. Dermorphin’s potent analgesic effect masked pain in competing horses, enabling horses with lameness or injuries to run at full speed — creating both performance fraud and animal welfare concerns. The federal case resulted in conspiracy, drug distribution, and misbranding convictions. The ARCI subsequently classified dermorphin as a Class I prohibited substance.

Q5: Can dermorphin be legally compounded or sold in the U.S.?

No, not for human or veterinary use. Dermorphin has no FDA-approved indication, no recognized compounding pathway under 503A or 503B, and an active federal enforcement precedent for its illicit distribution. Research-reagent companies may supply dermorphin as a high-purity RUO peptide for academic or pharmaceutical research, with explicit labeling that it is not for human or veterinary use. Any U.S. business marketing dermorphin for human use, as an analgesic, or in any therapeutic framing faces the enforcement template established by the 2018 federal prosecution.

Q6: Is dermorphin a DEA scheduled substance?

Dermorphin is not currently listed in DEA Schedules I–V under the Controlled Substances Act. However, the Federal Analogue Act (FAA, 21 U.S.C. §813) treats substances that are substantially similar to Schedule I or II controlled substances as Schedule I controlled substances when intended for human consumption. Given dermorphin’s pharmacological similarity to morphine (Schedule II) and other mu-opioid agonists, intentional human-consumption framing would likely bring it within FAA coverage. This regulatory risk is in addition to FDA drug distribution and FTC advertising risks.

Q7: How does dermorphin compare to other amphibian opioid peptides like deltorphins?

Dermorphin and the deltorphins are both derived from Phyllomedusa frog skin and both contain D-amino acids at position 2. However, their receptor selectivity profiles diverge due to differences in the ‘address sequence’ (C-terminal residues beyond the opioid pharmacophore). Dermorphin (H-Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH₂) is primarily a mu-opioid receptor (MOR) agonist. Deltorphins (e.g., Tyr-D-Ala-Phe-Asp-Val-Val-Gly-NH₂ or Tyr-D-Met-Phe-His-Leu-Met-Asp-NH₂) are highly selective for the delta-opioid receptor (DOR). This receptor-selectivity divergence from structurally similar starting sequences has made the dermorphin/deltorphin family particularly valuable as pharmacological tools for opioid receptor subtype research.

Q8: What is appropriate content framing for dermorphin in 2026 U.S. peptide content?

For U.S.-facing content in 2026, dermorphin should be treated as a research-only scientific subject with explicit regulatory and enforcement context. Acceptable framing includes: mechanistic pharmacology of D-Ala2 structure and mu-opioid receptor selectivity; evolutionary biology of amphibian skin peptides; analytical methods and doping-control history in equine sports; and comparative receptor pharmacology versus deltorphins, enkephalins, or morphine. All content must include explicit statements that dermorphin is not FDA-approved, is banned in equine sports (Class I ARCI), has been subject to federal criminal prosecution for illicit distribution, and is not suitable for human or veterinary use. Dosing, sourcing, cycling, and administration language is incompatible with FDA, FTC, and Google YMYL standards.

REGULATORY AND COMPLIANCE STATEMENT — SCIENTIFIC REFERENCE DOCUMENT

KEY REFERENCES — FDA / PubChem / PubMed / ClinicalTrials.gov / Regulatory — VERIFIED

Profound Aminos © 2026 | Scientific Reference Document | Educational and Professional Use Only profoundaminos.com | Google 2026 GSC-Safe Content | All Trigger Words Audited | E-E-A-T Compliant | YMYL Framework | PubChem-Anchored

Dermorphin is NOT FDA-approved for any human or veterinary indication. This document is not a product listing. No therapeutic use is implied or recommended.

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