Dermorphin 10 mg

Dermorphin is a naturally occurring heptapeptide opioid agonist research peptide first isolated from skin secretions of the South American amphibian Phyllomedusa sauvagei. The peptide sequence is H-Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH2, with the unusual D-alanine residue at position 2 distinguishing it from mammalian opioid peptides and contributing to its biological stability in research models. It is supplied as an investigational laboratory peptide for use in opioid-receptor signaling research and neuropeptide receptor binding studies.

Research interest in Dermorphin focuses on its role as a high-affinity, μ-opioid-receptor selective agonist used as a reference compound in receptor pharmacology research. Because dermorphin exhibits markedly higher μ-receptor selectivity than mammalian enkephalins and endorphins, it serves as a structural and pharmacological prototype for delta-opioid-receptor research peptide investigations and broader opioid-receptor signaling research in research models (Montecucchi et al., 1981, International Journal of Peptide and Protein Research).

In laboratory research studies, dermorphin is used to investigate μ-opioid-receptor binding kinetics, G-protein coupling, β-arrestin recruitment, and downstream second-messenger cascades. Comparative research with native enkephalins, endorphins, and deltorphin analogs supports laboratory research on opioid-receptor signaling research, peptide structure-activity relationships, and D-amino-acid-mediated enzymatic stability in research models. Dermorphin is also widely used as a tool for mapping opioid-receptor distribution in nervous-system tissue research and for investigating peptide pharmacokinetics in laboratory species.

The peptide is supplied as a lyophilized powder to ensure optimal stability during storage and handling.

Dermorphin was first isolated and characterized in 1981 from methanol extracts of the skin of Phyllomedusa sauvagei by Montecucchi, Erspamer, and colleagues. The peptide was identified as the prototype of a novel class of opioid peptides distinguished by the incorporation of a D-amino acid at position 2, produced through post-translational isomerization of encoded L-alanine by a specialized amino-acid isomerase in the frog's skin secretory granules.

The dermorphin sequence (H-Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH2) differs markedly from mammalian enkephalins and endorphins, lacking the traditional N-terminal Tyr-Gly-Gly-Phe motif. Despite this structural divergence, it binds with exceptionally high affinity and selectivity to μ-opioid receptors in research models. The D-Ala2 residue is essential for this activity in receptor-binding research, as replacement with L-alanine renders the peptide essentially inactive at the receptor.

Since its discovery, more than one hundred dermorphin analogs have been synthesized, establishing comprehensive structure-activity relationships for this peptide family. This positioning at the intersection of amphibian peptide chemistry, opioid-receptor signaling research, and neuropeptide receptor binding studies has made dermorphin a widely used reference compound in laboratory research models of opioid-receptor pharmacology.

1. μ-Opioid Receptor Engagement

Dermorphin is studied as one of the most potent and selective naturally occurring μ-opioid receptor agonists in research models. In receptor-binding research it demonstrates high affinity for μ-receptors with markedly lower affinity for δ- and κ-opioid receptor subtypes. This selectivity makes it a precision tool for opioid-receptor signaling research, G-protein coupling studies, and downstream intracellular pathway investigations.

2. Receptor-Signaling Cascades

Upon μ-opioid receptor engagement, dermorphin modulates Gαi/o-coupled signaling in research models, including inhibition of adenylyl cyclase activity, modulation of intracellular cyclic AMP, and activation of inwardly rectifying potassium channels. These cascades are widely investigated in neuropeptide receptor binding studies and opioid-receptor signaling research.

3. Enzymatic Stability via D-Ala2

The presence of the D-Ala2 residue confers resistance to degradation by mammalian aminopeptidases and endopeptidases in research models, resulting in prolonged engagement at the receptor compared to L-amino-acid opioid peptides. This property is investigated in laboratory research examining how D-amino-acid substitution influences peptide stability, blood-brain barrier permeability research, and duration of receptor occupancy in research models.

4. Structure-Activity Research

By systematic modification of the dermorphin sequence, including substitutions at positions 2, 4, and 6, truncation studies, and additional D-amino-acid replacements, researchers map the structural determinants of μ-receptor selectivity, binding affinity, and agonist efficacy. The N-terminal tetrapeptide (Tyr-D-Ala-Phe-Gly) has been identified in research models as the minimal sequence requirement for μ-opioid receptor engagement.

Research Applications

Conclusion

Dermorphin is a naturally occurring amphibian heptapeptide research compound investigated as a high-affinity, μ-selective opioid-receptor agonist in research models. Its incorporation of a D-alanine residue at position 2, a rare feature among vertebrate peptides, confers exceptional enzymatic stability and distinguishes it structurally from all mammalian opioid peptides. By serving as a prototype for a distinct class of opioid peptide research compounds, dermorphin provides a valuable research tool for opioid-receptor signaling research, neuropeptide receptor binding studies, and peptide structure-activity research in research models.

Research Use Disclaimer

This product is intended for research and laboratory use only. It is designed exclusively for in vitro research purposes. All information provided is for educational and research reference only. This product is not intended for human or animal use. It is not a drug, food, or cosmetic and must not be marketed, labeled, or used as such. Use and handling are restricted to trained and qualified professionals.