Dermorphin
Research Peptide | Lyophilized Powder | Batch Tested
For laboratory research use only. Not for human or animal consumption. Insulated shipping · Styrofoam box available.
Product Overview
Dermorphin is a naturally occurring heptapeptide originally isolated from the skin of South American frogs, and one of the most potent and selective μ-opioid receptor agonists known. It contains a rare D-amino acid that gives it high stability and potency.
| Test | Result | Status |
|---|---|---|
| Purity | 99.8% | Passed ✓ |
| Test | Result | Status |
|---|---|---|
| Purity | 99.9% | Passed ✓ |
| Test | Result | Status |
|---|---|---|
| Purity | 99.0% | Passed ✓ |
Research Information
Dermorphin is used as a research tool to study μ-opioid receptor signaling and analgesic (antinociceptive) pathways in laboratory models, where its extreme potency and enzymatic resistance make it valuable for characterizing opioid-receptor pharmacology. Supplied strictly for in-vitro and laboratory research use only — not for human or animal consumption.
Dermorphin Research & Studies
What is Dermorphin?
Dermorphin is a naturally occurring heptapeptide originally isolated from the skin secretions of certain South American frog species. In research settings it is recognized as one of the most potent and selective agonists of the μ-opioid receptor. The molecule incorporates a rare D-amino acid residue that contributes to its enzymatic stability and high receptor affinity. It is supplied exclusively for in-vitro and laboratory investigation of opioid receptor systems.
Mechanism of Action
In experimental systems Dermorphin binds with high affinity and selectivity to the μ-opioid receptor, a G-protein-coupled receptor. Receptor engagement activates intracellular signaling cascades that include inhibition of adenylyl cyclase and modulation of ion-channel activity. The D-alanine configuration stabilizes the bioactive conformation and prolongs receptor interaction relative to many endogenous opioid peptides. Investigators use these properties to map μ-receptor conformational dynamics and downstream pathways.
Primary Areas of Research
Dermorphin functions as a reference tool for characterizing μ-opioid receptor pharmacology in cellular and biochemical assays. Research focuses on ligand-binding kinetics, signal-transduction efficiency, and structure-activity relationships among opioid peptides. Its resistance to proteolytic degradation permits extended observation of receptor-mediated effects in vitro. Comparative studies also examine its selectivity profile against delta and kappa opioid receptor subtypes.
Key Research Findings
Receptor-binding and functional assays consistently show that Dermorphin exhibits exceptional potency and μ-selectivity compared with many classical opioid ligands. Structural work underscores the essential contribution of the D-amino acid to both affinity and metabolic stability. Laboratory models demonstrate prolonged receptor occupancy attributable to reduced enzymatic cleavage. These attributes render the peptide useful for dissecting opioid-receptor subtypes and allosteric modulation sites.
Research Handling & Considerations
As a research peptide, Dermorphin requires standard laboratory handling protocols appropriate for bioactive peptides. Storage conditions should be selected to maintain chemical integrity and biological activity for experimental use. All applications must remain confined to in-vitro systems and approved laboratory model platforms. Researchers are advised to confirm identity and purity before incorporation into receptor or signaling assays.
Frequently Asked Questions
Dermorphin is studied as a highly selective agonist of the μ-opioid receptor, showing minimal activity at other opioid receptor subtypes in binding assays.
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