Dermorphin | Heptapeptide Chemical Reference Material
Chemical Identity
- CAS: 77614-16-5
- PubChem: Base peptide CID 5485199; acetate CID 163335308
- Listed base formula: C40H50N8O10
- Listed base molecular weight: 802.88 g/mol
- Sequence: H-Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH₂
- Length: Seven residues
- N-terminus: Free amine
- C-terminus: Primary amide, Ser7-NH₂
- Stereochemical feature: D-alanine at position 2
- Biological origin reference: Phyllomedusa sauvagei skin secretions and related amphibian peptides
For laboratory research use only. Not for use in humans or animals.
Molecular Research Context
Dermorphin is a heptapeptide associated with μ-opioid receptor (MOR/OPRM1) research. D-Ala2, the Tyr1 aromatic group, Pro6 conformation, and C-terminal amidation provide structural contexts for ligand binding and enzymatic susceptibility measurements.
The listed sequence is the primary identity reference. The original page’s one-letter notation does not agree with its seven-residue sequence and should not be used for identity calculations. Confirm sequence, stereochemistry, salt form, and molecular mass using material documentation.
Structure-Activity Assays
- D-Ala2 and L-Ala2 scaffold measurements in receptor-binding assays
- Tyr1-D-Ala2 ligand-contact analysis
- Amidated and free-acid terminal-form characterization
- Pro6 cis/trans conformation and C-terminal sequence measurements
- Aminopeptidase, DPP-4, and carboxypeptidase susceptibility assays
Related amphibian peptides such as deltorphins provide distinct molecular contexts for μ, δ, and κ receptor interaction studies. Selectivity and activity depend on molecular identity and experimental conditions.
Receptor Signaling Measurements
MOR is a class A GPCR. Laboratory endpoints include Gi/Go-associated signaling, adenylyl-cyclase activity, cAMP measurements, GIRK channel readouts, calcium-channel responses, and transmitter-release assays. Use receptor-expression data and appropriate assay controls when interpreting these endpoints.
The existing literature describes guinea-pig ileum and mouse vas-deferens ex-vivo assay contexts. These systems provide functional readouts for receptor-pathway research. Antagonist controls, including naloxone in the cited methods, provide experimental context without establishing a general material outcome.
Molecular Structure
The retained structure image represents the listed heptapeptide sequence. Acetate and base-peptide records are separate material identities and require salt-correct mass calculations.
Analytical Characterization
Research contexts include peptide sequence mapping, stereochemical confirmation, intact-mass analysis, degradation-fragment profiling, and LC-MS/MS measurements in validated matrices. The existing method discussion reports sensitivity as low as 2 pg/mL in serum; confirm extraction, ion assignment, instrument settings, and validation conditions in the original method.
Laboratory Handling
Use appropriate laboratory PPE and follow institutional safety procedures for receptor-active peptide materials. Consult available material safety and batch documentation before handling. Storage, solvent selection, and stability conditions should follow the supplied material’s documented specifications.
Existing Scientific Reference Identifiers
The existing bibliography identifies Montecucchi et al., PMID 7264829; Melchiorri and Negri, PMID 8981054; Negri et al., PMID 11090648; Erspamer et al., PMID 2544892; Kreil et al., PMID 2759166; Terenius, PMID 4801733; Corbett et al., PMID 16402099; and Melchiorri et al., PMID 3027213. Consult original records for exact molecular forms, receptor systems, and analytical endpoints.
For laboratory research use only. Not for use in humans or animals.

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