Description
Dermorphin is a naturally occurring peptide originally isolated from the skin secretions of South American tree frogs of the Phyllomedusa genus. Known for its powerful bioactive properties, Dermorphin has attracted significant interest in the scientific community due to its unique structure and high affinity for specific opioid receptors.
This peptide is recognized for its ability to bind to the mu-opioid receptor with remarkable selectivity, which results in effects far more potent than morphine on a per-weight basis in research settings. Because of this, Dermorphin has become a subject of investigation for its potential roles in pain modulation, neurobiology, and receptor signaling.
Key features include:
-
High receptor affinity – Dermorphin demonstrates strong binding at the mu-opioid receptor, making it a valuable research tool for understanding opioid pathways.
-
Enhanced potency – Studies suggest it is significantly more potent than morphine in experimental models.
-
Unique peptide structure – Its amino acid sequence includes a rare D-amino acid, contributing to its unusual stability and activity profile.
-
Research applications – Investigated for its role in analgesia, neurochemical signaling, and peptide-receptor interactions.


