Dermorphin 5mg

Dermorphin is a naturally occurring opioid peptide originally identified in the skin secretions of certain South American frog species and now produced synthetically for laboratory research. It is studied in receptor pharmacology research as a reference ligand for the mu-opioid receptor, valued in research settings for its high binding affinity and receptor selectivity compared to many other opioid peptides.

What Is Dermorphin?

Structurally, dermorphin is a short peptide containing a D-amino acid, a feature rarely found in mammalian peptides and one that contributes to its resistance to enzymatic breakdown in research models. This structural stability, combined with its receptor-binding profile, is why dermorphin is used in laboratory settings as a pharmacological tool compound rather than as a subject studied for its own biological origin.

Ingredients

• Dermorphin (H-Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH2)

Dermorphin is supplied as a single-component lyophilized peptide. No additional active ingredients are present in this formulation.

Dermorphin Research Areas

Dermorphin and Opioid Receptor Binding

Research has examined dermorphin’s binding affinity at the mu-opioid receptor, using it as a reference compound to characterize receptor structure and ligand-binding behavior in cell-based and biochemical assay models.

Dermorphin and Receptor Selectivity Research

Studies have investigated dermorphin’s selectivity for the mu-opioid receptor relative to other opioid receptor subtypes, contributing to broader research on receptor-subtype-specific pharmacology.

Dermorphin and Peptide Structure-Activity Studies

Because dermorphin contains a D-amino acid residue, it has been used in structure-activity research examining how amino acid configuration affects peptide stability, receptor binding, and resistance to enzymatic degradation.

Mechanism of Action

Dermorphin is studied for its high-affinity interaction with the mu-opioid receptor, a G protein-coupled receptor involved in opioid receptor signaling pathways. Its D-amino acid residue is of particular research interest, as this configuration is associated with increased resistance to peptidase degradation relative to standard L-amino acid peptides, a property studied in the context of peptide stability and structure-activity relationships. Research using dermorphin contributes to the broader scientific understanding of opioid receptor pharmacology and ligand design.

Specifications

For laboratory research use only. Not for human or animal use. Not intended to diagnose, treat, cure, or prevent any disease. Restricted to qualified laboratory research personnel.