What is Dermorphin?
Dermorphin is a naturally occurring opioid heptapeptide (seven amino acids) with the sequence Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH2. It is notable for containing a D-alanine residue at position two, an unusual feature that gives the peptide resistance to enzymatic breakdown. Dermorphin was first isolated from the skin of South American frogs of the genus Phyllomedusa. GenoPept supplies Dermorphin in the UK as a lyophilised powder for laboratory research.
Dermorphin is studied as a potent and selective agonist at the mu-opioid receptor, and is used as a reference ligand in opioid-receptor pharmacology. Its natural D-amino-acid content makes it a frequently cited example of a stabilised bioactive peptide in the research literature.
Dermorphin research applications
Preclinical research on Dermorphin covers several model-based areas, listed here for scientific context only.
- Opioid-receptor pharmacology: studied as a selective mu-opioid receptor agonist in binding assays.
- Analgesia models: investigated in animal models of nociception.
- Peptide stability: examined as a D-amino-acid-containing peptide resistant to degradation.
- Structure-activity studies: used as a template in opioid peptide structure-activity research.
Mechanism of action (preclinical)
In preclinical studies, Dermorphin is reported to act as a high-potency, high-selectivity agonist at the mu-opioid receptor, a G-protein-coupled receptor. Activation of this receptor in model systems is reported to inhibit adenylate cyclase and modulate ion-channel activity in neurons. The D-alanine residue at position two protects the peptide from peptidase cleavage, which contributes to its reported potency in assays. Because of this selectivity, Dermorphin is often used as a positive control alongside non-selective opioid ligands in comparative binding studies. These are laboratory observations only and are not statements about effects in people.
Dermorphin product specifications
| Compound | Dermorphin |
|---|---|
| Also known as | Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH2 |
| Sequence / class | Opioid heptapeptide (Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH2) |
| CAS number | 77614-16-5 |
| Molecular formula | C40H50N8O10 |
| Molecular weight | 802.9 g/mol |
| Form | Lyophilised powder |
| Available sizes | 5 mg, 10 mg |
| Purity | ≥99% (HPLC) |
| Verification | HPLC purity + LC-MS identity, third-party (ISO/IEC 17025) |
| Storage (unopened) | –20 °C long term, protected from light |
| Intended use | In-vitro laboratory research only |
Available sizes
- Dermorphin 5mg vial
- Dermorphin 10mg vial
Dermorphin is offered in the vial sizes listed above for UK research laboratories. Wholesale boxes of 10 vials are available through GenoPept for teams running larger studies, with tiered savings on bulk orders. See the bulk and wholesale page for details.
Reconstitution, handling and storage (laboratory)
Dermorphin is supplied as a lyophilised (freeze-dried) powder in a sealed sterile glass vial with a black cap. For laboratory reconstitution, add bacteriostatic water or a suitable sterile diluent slowly down the inner vial wall, then swirl gently until dissolved. Never shake the vial, as agitation can shear the peptide.
Store unopened vials at –20 °C for long-term stability, or at 2–8 °C for short periods, protected from light. After reconstitution, keep the solution at 2–8 °C and use it within the window stated in the laboratory protocol. See the GenoPept guides on how to reconstitute research peptides and how to store research peptides.
Quality assurance and Certificate of Analysis
Every batch of Dermorphin supplied by GenoPept is verified to at least 99% purity. Identity and purity are confirmed by an independent third-party laboratory (Puralytix, accredited to ISO/IEC 17025) using HPLC for purity and LC-MS for identity. Each vial is batch-identified with a lot number and expiry date on the label.
The matching Certificate of Analysis (COA) is available from the “View Certificate of Analysis” button on this page, and the full library is published at the GenoPept COA certificates page. Learn more about what a Certificate of Analysis shows and the UK legal status of research peptides.
Related research compounds
- PT-141 (Bremelanotide) — a melanocortin peptide studied in behavioural research.
- Oxytocin — a neuropeptide studied in social behaviour research.
- Selank — a tuftsin-derived anxiolytic research peptide.
- Semax — a nootropic ACTH(4-10) research peptide.
Dermorphin frequently asked questions
What is Dermorphin used for in research?
Dermorphin is used in laboratory research to study mu-opioid receptor pharmacology, nociception models, peptide stability and opioid structure-activity relationships. As a potent, selective mu-opioid agonist it is a common reference ligand in binding assays. It is supplied strictly for in-vitro research and is not intended for human use, diagnosis or therapy.
How is Dermorphin supplied and what is its purity?
GenoPept supplies Dermorphin as a lyophilised powder in sealed sterile glass vials with black caps, in 5 mg and 10 mg sizes. Every batch is verified to at least 99% purity by an independent ISO/IEC 17025 laboratory using HPLC and LC-MS, and each order includes a batch Certificate of Analysis available from the product page.
How should Dermorphin be stored?
Store unopened Dermorphin vials at –20 °C for long-term stability, or at 2–8 °C for short periods, protected from light. After reconstitution with bacteriostatic water or sterile diluent, keep the solution at 2–8 °C and use it within the window stated in the laboratory protocol to preserve peptide integrity.
Is Dermorphin for human use?
No. Dermorphin from GenoPept is a research chemical supplied for in-vitro laboratory research only. It is not a medicine, not for human or veterinary use, and not intended for diagnostic or therapeutic purposes. All handling should be carried out by qualified personnel in a controlled laboratory setting in line with UK research guidance.
What makes Dermorphin unusual among peptides?
Dermorphin contains a D-alanine residue at position two, whereas most natural peptides are built only from L-amino acids. This D-amino-acid substitution makes the peptide resistant to enzymatic breakdown and contributes to its high potency and selectivity at the mu-opioid receptor, which is why it is widely studied in opioid research.
Research use only. This product is supplied for in-vitro laboratory research only. It is not for human or veterinary use, is not a medicine, and is not intended for diagnostic or therapeutic use. Handling should be carried out only by qualified personnel in an appropriate laboratory setting.
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