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Compound guide
Dermorphin: what the research covers
A seven-residue opioid peptide from amphibian skin, and one of the few natural peptides containing a D-amino acid. That single unusual residue is the reason it works at all.
What Dermorphin is
Dermorphin was isolated from the skin of South American tree frogs of the genus Phyllomedusa, and its sequence is Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH2. The second residue is D-alanine, which is remarkable: ribosomal protein synthesis produces L-amino acids, so a natural peptide containing a D residue implies post-translational enzymatic inversion. Very few are known.
That inversion is not decoration. D-alanine at position two blocks the aminopeptidase cleavage that would otherwise destroy the peptide immediately, and it also shapes the conformation that the receptor recognises. Synthetic peptide chemists arrived at the same trick independently — the D-alanine in GHRP-2 is there for the same reason.
Pharmacologically it is a mu-opioid receptor agonist with high affinity and unusually high selectivity over the delta and kappa subtypes.
Why it is used as a pharmacological tool
The opioid receptor family is closely related, and separating mu-mediated effects from delta- and kappa-mediated ones is a recurring methodological problem. Most classical agonists are imperfectly selective, so an observation can rarely be assigned to one subtype with confidence. Dermorphin selectivity is high enough that it became a reference mu agonist in receptor pharmacology for exactly that reason.
The literature therefore runs through receptor binding and subtype selectivity assays, G-protein coupling and beta-arrestin recruitment, structure-activity work on the D-alanine position and on the C-terminal amide, and the broader question of how amphibian skin peptides relate to the mammalian endogenous opioid system.
It belongs in the repair group in this catalogue only loosely. Its scientific home is receptor pharmacology, and it is listed here because its tissue origin and its antinociceptive literature sit closer to that group than to any other.
How Amino Club supplies it
Supplied lyophilised in sealed vials as Dermorphin, specified at 99% purity or better by HPLC with identity confirmed by mass spectrometry and released against the Certificate of Analysis for its own batch, as set out on the lab testing page.
Identity confirmation carries real weight on this molecule. The all-L version of the same sequence is a different compound with a fraction of the activity, and it has the same mass — so stereochemistry is established by synthesis route and chromatographic behaviour rather than by mass alone, which is one reason batch documentation matters. The dry powder is stored below −18 °C and solutions prepared in small volumes; diluents are under reconstitution supplies.
Because this is an opioid receptor agonist, local rules on its possession and use may differ from those applying to the rest of the catalogue. Confirming the position in your own jurisdiction before ordering is the buyer responsibility.
Related reading
Dermorphin is listed in the tissue repair research peptides group alongside BPC-157, TB-500, ARA-290, KPV, LL-37 and VIP, though its own literature is receptor pharmacology rather than repair.
Every guide is indexed in the research library. Certificates and storage are covered on the FAQ, quantity pricing through bulk and wholesale.
Research use only
Dermorphin supplied by Amino Club is a laboratory reference material. It is not a medicine, not a supplement, and not for human or veterinary use, and no dosing guidance or administration protocol is provided. The full terms are in the research use policy.