Structure
Dermorphin does not contain the common N-terminal sequence for the traditional endogenous opioid peptides (Tyr–Gly–Gly–Phe), and its sequence is completely different from those of the endomorphins, which were identified as endogenous μ-opioid peptides that also do not contain the common sequence. Interestingly, DM contains D-alanine (a D-isomer amino acid) in its sequence. The primary structure of dermorphin is YDAFGYPS-NH2.
Description
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.
Uses
A mu-opioid receptor agonist
Definition
ChEBI: Dermorphin is an oligopeptide.
Side effects
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].
in vitro
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.
References
[1] Negri, L. P. Melchiorri and R. Lattanzi. “Opioid and Bv8 Peptides.”Handbook of Biologically Active Peptides (Second Edition) 2013:376-383.
