Compound monograph
Dermorphin
Dermorphin is a seven-residue peptide with D-alanine at position 2, an uncapped N-terminus and a C-terminal amide. This record describes the neutral parent separately from modified derivatives and counterion-containing preparations.
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Identity & nomenclature
Dermorphin is a seven-residue peptide with D-alanine at position 2, an uncapped N-terminus and a C-terminal amide. This record describes the neutral parent separately from modified derivatives and counterion-containing preparations.
The PubMed abstract of Montecucchi et al. (1981; PMID 7287299) prints Try at the first position, while the publisher abstract for DOI 10.1111/j.1399-3011.1981.tb01993.x prints Tyr. This record follows the publisher-supported Tyr sequence; the indexed Try spelling is retained here as a noted transcription error.
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Molecular properties
| Molecular formula | C40H50N8O10 |
|---|---|
| Molecular mass | 802.886 Da |
| CAS Registry Number | 77614-16-5 |
| PubChem CID | 5485199 |
| UNII | 2SEC01B703 |
| Three-letter sequence | Tyr–D-Ala–Phe–Gly–Tyr–Pro–Ser |
| Terminal groups | Free N-terminal amino group; C-terminal amide |
Residues are numbered from the N-terminus. Ala2 is D; Tyr1, Phe3, Tyr5, Pro6 and Ser7 are L; Gly4 is achiral. No one-letter string is supplied because it would conceal D-alanine at position 2.
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Structural characteristics
Linear seven-residue peptide; no interresidue covalent ring closure is specified. Sachon et al. compared prepared peptide isomers by mass spectrometry. Pang et al. independently examined dermorphin monomers and oligomers by ion-mobility mass spectrometry. Preparation-level stereochemical and counterion limitations remain specific to those studies.
- D-alanine at position 2
Terminal features: Free N-terminal amino group, C-terminal amide.
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Molecular targets & mechanisms
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Analytical considerations
No compound-specific analytical note is recorded for this compound; identifier and bibliography verification remain available below.
What the studies reported
No verified findings are published for this record under Content Policy v1.
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Verified bibliography
Cited studies by type
The 2 papers this record cites, counted by the kind of work each reports. A count is the size of this record's selection, not of the research that exists, and says nothing about results, safety, effectiveness or approval.
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Reference 1
D-amino acid detection in peptides by MALDI-TOF-TOF.Sachon E, Clodic G, Galanth C, Amiche M, Ollivaux C, Soyez D, Bolbach G
Analytical chemistry · 2009-06-01 · Journal Article
currentReference 2
Structural Characterization of Monomers and Oligomers of D-Amino Acid-Containing Peptides Using T-Wave Ion Mobility Mass Spectrometry.Pang X, Jia C, Chen Z, Li L
Journal of the American Society for Mass Spectrometry · 2016-11-07 · Journal Article
current
Study models of these references
What kind of experiment each cited paper reports, taken from its abstract unless marked. Not a summary of results.
| Reference | Study models |
|---|---|
| Sachon E et al. 2009 | Chemical, structural or analytical study; no biological model reported |
| Pang X et al. 2016 | Chemical, structural or analytical study; no biological model reported |
Record history
Published 2026-10-20.
- : Identity and nomenclature, Sequence and structure, Analytical notes
Each entry names the parts of this record that changed on that date. Changes to links between records and to catalogue links are not listed. This history covers the tracked record fields; study findings are not listed here.
Cite this record: Purely Peptides Research Library. Dermorphin. Published 2026-10-20; updated 2026-10-20. https://purelypeptides.org/research/compounds/dermorphin/
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Methodology & citation verification
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