Dermorphin is a seven-amino acid opioid peptide originally isolated from the skin of South American frogs (Phyllomedusa). It is one of the most potent naturally occurring mu-opioid receptor agonists, with approximately 30-40 times the potency of morphine. It contains the rare D-alanine amino acid, making it resistant to enzymatic degradation.
| Sequence / Structure | Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH2 |
| Molecular Weight | 803.92 g/mol |
| Purity | >=98% |
| Appearance | White lyophilized powder |
| Storage | Store at -20C, reconstituted at 2-8C |
| Solubility | Soluble in water |
Montecucchi PC, de Castiglione R, Piani S, et al. (1981) — Amino acid composition and sequence of dermorphin, a novel opiate-like peptide from the skin of Phyllomedusa sauvagei. Int J Pept Protein Res. DOI: 10.1111/j.1399-3011.1981.tb01993.x
Erspamer V, Melchiorri P, Falconieri-Erspamer G, et al. (1989) — Deltorphins: a family of naturally occurring peptides with high affinity and selectivity for delta opioid binding sites. Proc Natl Acad Sci USA. DOI: 10.1073/pnas.86.13.5188
Negri L, Lattanzi R, Tabacco F, et al. (1999) — Dermorphin and deltorphin glycosylated analogues: synthesis and antinociceptive activity after systemic administration. J Med Chem. DOI: 10.1021/jm9811197
A potent seven-amino acid opioid peptide from frog skin, 30-40x more potent than morphine at mu-opioid receptors.
The D-Ala at position 2 confers resistance to aminopeptidase degradation and is unique among naturally occurring opioid peptides.
>=98% with full analytical documentation.
Mu-opioid pharmacology, pain research, analgesic development, and D-amino acid peptide studies.
Lyophilized at -20C, reconstituted at 2-8C.
Yes, competitive bulk pricing available.
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