Dermorphin

Dermorphin first isolated from skin extracts of the South American frog Phyllomedusa sauvagei, corresponds to the predicted prodermorphin heptapepeptide. It acts as a highly potent and fully selective agonist for the δ-opioid receptor.

Dermorphin is a synthetic research peptide in the dermorphin / mu-opioid peptide family. Dermorphin is a heptapeptide originally isolated from Phyllomedusa frog skin and is distinguished by a D-Ala residue at position 2. Published pharmacology established dermorphin as a potent opioid peptide, and later structure-activity work showed that the N-terminal tetrapeptide contains the minimal sequence required for strong mu-opioid receptor agonism. D-Arg and other substitutions have been used to modify enzymatic stability and receptor pharmacology.

• mu-opioid receptor binding assays
• opioid peptide structure-activity studies
• agonist potency comparisons
• metabolic-stability experiments

The exact sequence, reporter group, phosphorylation state, stereochemistry, and terminal modifications should be considered when comparing this reagent with the parent peptide or published assay substrates. Enzyme concentration, buffer composition, cofactors, pH, ionic strength, and substrate concentration can also affect measured activity.

1. Pharmacological data on dermorphins, a new class of potent opioid peptides from amphibian skin
2. Dermorphin tetrapeptide analogs as potent and long-lasting analgesics