SingleCognitive & Sleep

Dermorphin 5mg

Natural amphibian heptapeptide exhibiting exceptional mu-opioid receptor affinity and metabolic stability via an unusual D-amino acid.

Mechanism

Dermorphin binds selectively and with high affinity to mu-opioid receptors, triggering profound downstream G-protein-mediated antinociceptive and depressant signaling pathways resistant to typical peptide cleavage.

Dosing

Published experimental references outline a starting research handling concentration baseline of 100 mcg (4 units on a U-100 syringe).

Reconstitution

Reconstituting a 5 mg vial with 2.0 mL of bacteriostatic water yields an analytical research concentration of 2.5 mg/mL.

Storage

Store the unmixed powder or refrigerated reconstituted solution between 2 and 8 °C, shielded from ambient light, and do not freeze the liquid form.

Mix & measure Dermorphin 5mg

Pre-filled with this protocol's recommended BAC water and documented starting dose — edit any field to run your own numbers.

Mix & measure Dermorphin 5mg

Vial strength → BAC water → target dose

Vial strength

BAC water

Target dose

Concentration2.50mg/mL

Draw volume0.040mL

On the syringe4.00units

Total doses in vial: 50.0

100u80u60u40u20u0

U-100 syringe: 100 units = 1 mL

Reconstitution math only — not dosing advice. U-100 syringe: 100 units = 1 mL. Advanced calculator →

Dosing Chart

Phase / Day(s)	Dose & Frequency	Volume (U-100 units / mL)
Reference Baseline	100 mcg experimental amount	4 units (0.04 mL)
Intermediate Reference	250 mcg experimental amount	10 units (0.10 mL)
Moderate Reference	500 mcg experimental amount	20 units (0.20 mL)
High Reference	1 mg experimental amount	40 units (0.40 mL)

Reconstitution Steps

1
Clean the rubber septums of the Dermorphin vial and bacteriostatic water vial with sterile alcohol swabs, allowing them to fully dry.
2
Draw 2.0 mL of bacteriostatic water using an appropriate reconstitution syringe.
3
Insert the needle at a slight angle and direct the stream gently down the glass wall of the vial to minimize agitation.
4
Allow the solution to settle for 30 seconds, then gently swirl the vial until the lyophilized cake is fully dissolved without vigorous shaking.
5
Verify the solution is clear and particulate-free, then refrigerate the vial at 2–8 °C away from light.

Supplies Needed

Peptide Vial

Contains 5 mg of lyophilized Dermorphin research powder

Insulin Syringes (U-100)

Calibrated syringes used to accurately measure small microliter volumes from the 2.5 mg/mL solution

Bacteriostatic Water

Sterile diluent (2.0 mL required) containing 0.9% benzyl alcohol for dissolving the lyophilized cake

Alcohol Swabs

Used to decontaminate rubber stoppers and maintain aseptic bench conditions prior to reconstitution

Why researchers study it

High-affinity mu-opioid receptor biology

Analgesic potency and antinociceptive pathways

Post-translational D-amino acid enzymatic resistance

Equine anti-doping forensic assay development

These describe what is being studied, not proven benefits, approved uses, or promised results.

Overview

Dermorphin is a naturally derived heptapeptide originally isolated from the skin secretions of the South American frog Phyllomedusa sauvagei. It holds a distinct place in peptide biochemistry due to the inclusion of a D-alanine residue at the second position, a modification created post-translationally from an L-alanine gene sequence. This structural hallmark confers strong protection against common proteolytic enzymes, allowing the molecule to maintain stability far beyond typical endogenous mammalian opioids. In experimental pharmacology, dermorphin acts as an exceptionally potent agonist at central and peripheral mu-opioid receptors. Preclinical animal evaluations demonstrate analgesic potencies significantly exceeding that of morphine, alongside marked central nervous system effects such as catalepsy, altered carbon dioxide sensitivity, and respiratory depression at higher concentrations. While these properties make it a classic pharmacological tool for dissecting opioid receptor dynamics, its potency also brings classical opioid-related toxicities. Dermorphin is strictly an experimental reagent intended for in vitro assays and animal pharmacology models. It is not approved for therapeutic administration in humans or clinical veterinary medicine. Outside legitimate biochemical exploration, its primary contemporary notoriety stems from illicit veterinary doping in competitive equine racing, prompting specialized analytical detection methods across anti-doping bodies.

References

1.Montecucchi et al., International Journal of Peptide and Protein Research, 1981 — Amino acid composition and sequence of dermorphin, a novel opiate-like peptide from the skin of Phyllomedusa sauvagei
2.Richter et al., Science, 1987 — D-alanine in the frog skin peptide dermorphin is derived from L-alanine in the precursor
3.Negri et al., PNAS, 1992 — Dermorphin-related peptides activate two mu opioid receptor subtypes that modulate antinociception and catalepsy in the rat
4.Melchiorri & Negri, General Pharmacology, 1996 — The dermorphin peptide family
5.Negri et al., British Journal of Pharmacology, 1998 — Respiratory and cardiovascular effects of the mu-opioid receptor agonist [Lys7]dermorphin in awake rats
6.Richards et al., Bioanalysis, 2013 — Detection and quantification of dermorphin and selected analogs in equine urine