Dermorphin was first isolated from the skin of the skin of South American frogs of the genus Phyllomedusa. It is a high potency natural opiate peptide that binds selectively to mu-opioid receptors.
A mu-opioid receptor agonist
ChEBI: Dermorphin is an oligopeptide.
Like μ-opiate agonists, dermorphins produce antinociception and also catalepsy, respiratory depression, constipation, tolerance, and dependence, although at a lower degree than morphine does[1].
Dermorphin, a peptide isolated from the skin of Phyllomedusa frogs and the peptide receptor (NOP) component by the endogenous agonist nociceptin/orphanin FQ (N/OFQ). In displacement binding studies at CHOhMu, Dermorphin and DeNo displac the binding of [3H]-DPN in a concentration dependent and saturable manner. Dermorphin displays an affinity of 7.17, while N/OFQ fails to displace [3H]-DPN at the Delta receptor. Dermorphin and DeNo stimulate the binding of GTPγ[35S] in a concentration dependent and saturable manner at the Mu receptor.
[1] Negri, L. P. Melchiorri and R. Lattanzi. “Opioid and Bv8 Peptides.”Handbook of Biologically Active Peptides (Second Edition) 2013:376-383.
