Dermorphin
Sequence-Defined Heptapeptide | Amphibian-Skin Peptide Research Reference | μ-Opioid Receptor Research Tool
H-Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH₂ | CAS 77614-16-5 | PubChem CID 5485199
FOR LABORATORY RESEARCH USE ONLY.
Not intended for use in humans or animals. No medical, veterinary, consumer, or sport-related application is represented. For qualified laboratory personnel in controlled research settings only.
Product Overview
Dermorphin is a sequence-defined oligopeptide originally identified in amphibian-skin peptide research. Its seven-residue sequence is H-Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH₂. Notably, the structure includes D-alanine at position 2, making it a useful reference material for studies involving peptide chirality, receptor-binding behavior, and structure–activity relationships.
Published literature has examined Dermorphin in relation to μ-opioid receptor binding. Accordingly, the page should remain limited to chemical identity, sequence information, quality documentation, and neutral receptor-research context.
Technical Specifications
| Parameter | Specification |
|---|---|
| Product Reference | Dermorphin |
| Material Category | Sequence-defined heptapeptide |
| Full Sequence | H-Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH₂ |
| Short Sequence | Y-{D-Ala}-FGYPS-NH₂ |
| Molecular Formula | C₄₀H₅₀N₈O₁₀ |
| Molecular Weight | Approximately 802.9 g/mol |
| CAS Number | 77614-16-5 |
| PubChem CID | 5485199 |
| Distinct Structural Feature | D-alanine residue at position 2 |
| Research Context | Peptide chirality, receptor binding, μ-opioid receptor research, structure–activity studies |
| Purity | Confirm from batch-specific Certificate of Analysis |
| Supply Format | Confirm from supplier documentation |
| Storage Conditions | Follow the batch-specific Certificate of Analysis |
| CoA Availability | Required for batch-level verification |
The Dermorphin identity data above is supported by PubChem and published peptide literature.
Research Context
Dermorphin is useful as a laboratory reference for sequence analysis, peptide chirality studies, receptor-binding assays, and comparative peptide-structure research. In addition, its D-alanine residue offers a clear structural feature for academic discussion of naturally occurring peptides containing D-amino acids.
Compliance Statement
Dermorphin is listed here exclusively as a laboratory research material. This page does not provide personal-use instructions, preparation steps, administration guidance, or consumer-facing claims.




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