Structure via PubChem · Public domain (PubChem)
dermorphin
Sign in to saveDermorphin is a hepta-peptide first isolated from the skin of South American frogs belonging to the genus Phyllomedusa. The peptide is a natural opioid that binds as an agonist with high potency and selectivity to mu opioid receptors. Dermorphin is about 30–40 times more potent than morphine. The amino acid sequence of dermorphin is H-Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH2.
Chemical data
- Formula
- C40H50N8O10
- Molecular weight
- 802.9 g/mol
- IUPAC name
- (2S)-N-[(2S)-1-amino-3-hydroxy-1-oxopropan-2-yl]-1-[(2S)-2-[[2-[[(2S)-2-[[(2R)-2-[[(2S)-2-amino-3-(4-hydroxyphenyl)propanoyl]amino]propanoyl]amino]-3-phenylpropanoyl]amino]acetyl]amino]-3-(4-hydroxyphenyl)propanoyl]pyrrolidine-2-carboxamide
via PubChem
Drug data · ChEMBL
- Molecule type
- Protein
via ChEMBL · EBI
Research
586 papers- Dermorphin tetrapeptide analogs as potent and long-lasting analgesics with pharmacological profiles distinct from morphine.Peptides · 2011
- The dermorphin peptide family.General pharmacology · 1996
- Dermorphin [D-Arg2, Lys4] (1-4) Amide Attenuates Burn Pain by Inhibiting TRPV1/NR2B Mediated Neuroinflammatory Signalling.Molecular neurobiology · 2025
- Dermorphin: A Missed Palliative Care Opportunity for Intrathecal Therapy in Oncological Patients?Pain medicine (Malden, Mass.) · 2019
- Rediscovery of old drugs: the forgotten case of dermorphin for postoperative pain and palliation.Journal of pain research · 2018
via PubMed
Wikidata facts
- Mass
- 802.365
Show 4 more facts
- chemical formula
- C₄₀H₅₀N₈O₁₀
- canonical SMILES
- CC(C(=O)NC(CC1=CC=CC=C1)C(=O)NCC(=O)NC(CC2=CC=C(C=C2)O)C(=O)N3CCCC3C(=O)NC(CO)C(=O)N)NC(=O)C(CC4=CC=C(C=C4)O)N
- isomeric SMILES
- C[C@H](C(=O)N[C@@H](CC1=CC=CC=C1)C(=O)NCC(=O)N[C@@H](CC2=CC=C(C=C2)O)C(=O)N3CCC[C@H]3C(=O)N[C@@H](CO)C(=O)N)NC(=O)[C@H](CC4=CC=C(C=C4)O)N
- Commons category
- Dermorphin
Sources (3)
via Wikidata · CC0
~1 min read
Article
3 sectionsContents
- Illicit use
- See also
- References
Dermorphin is a hepta-peptide first isolated from the skin of South American frogs belonging to the genus Phyllomedusa. The peptide is a natural opioid that binds as an agonist with high potency and selectivity to mu opioid receptors. Dermorphin is about 30–40 times more potent than morphine. The amino acid sequence of dermorphin is H-Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH2.
Dermorphin is not found in humans or other mammals and similar D-amino acid peptides have only been found in bacteria, amphibians, and molluscs. Dermorphin appears to be made in these through an unusual posttranslational modification carried out by an amino acid isomerase. This unusual process is needed because the D-alanine in this peptide is not among the 20 amino acids coded for in the genetic code and thus the peptide cannot be synthesized in the usual way from the encodings in the genome of an organism.