Dermorphin

Dermorphin is a hepta-peptide first isolated from the skin of South American frogs belonging to the genus Phyllomedusa.^[1] The peptide is a natural opioid that binds as an agonist with high potency and selectivity to mu opioid receptors.^[2][3] Dermorphin is about 30–40 times more potent than morphine.^[4] The amino acid sequence of dermorphin is H-Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH₂.

Dermorphin

Names
Other names Tyrosyl-alanyl-phenylalanyl-glycyl-tyrosyl-prolyl-serinamide
Identifiers
CAS Number	77614-16-5 Y
3D model (JSmol)	Interactive image
ChEMBL	ChEMBL278789 N
ChemSpider	4588650 N
PubChem CID	5485199
UNII	2SEC01B703 Y
CompTox Dashboard (EPA)	DTXSID40228281
InChI InChI=1S/C40H50N8O10/c1-23(44-37(55)29(41)18-25-9-13-27(50)14-10-25)36(54)46-30(19-24-6-3-2-4-7-24)38(56)43-21-34(52)45-31(20-26-11-15-28(51)16-12-26)40(58)48-17-5-8-33(48)39(57)47-32(22-49)35(42)53/h2-4,6-7,9-16,23,29-33,49-51H,5,8,17-22,41H2,1H3,(H2,42,53)(H,43,56)(H,44,55)(H,45,52)(H,46,54)(H,47,57)/t23-,29+,30+,31+,32+,33+/m1/s1 N Key: FHZPGIUBXYVUOY-VWGYHWLBSA-N N InChI=1/C40H50N8O10/c1-23(44-37(55)29(41)18-25-9-13-27(50)14-10-25)36(54)46-30(19-24-6-3-2-4-7-24)38(56)43-21-34(52)45-31(20-26-11-15-28(51)16-12-26)40(58)48-17-5-8-33(48)39(57)47-32(22-49)35(42)53/h2-4,6-7,9-16,23,29-33,49-51H,5,8,17-22,41H2,1H3,(H2,42,53)(H,43,56)(H,44,55)(H,45,52)(H,46,54)(H,47,57)/t23-,29+,30+,31+,32+,33+/m1/s1 Key: FHZPGIUBXYVUOY-VWGYHWLBBR
SMILES C[C@H](C(=O)N[C@@H](CC1=CC=CC=C1)C(=O)NCC(=O)N[C@@H](CC2=CC=C(C=C2)O)C(=O)N3CCC[C@H]3C(=O)N[C@@H](CO)C(=O)N)NC(=O)[C@H](CC4=CC=C(C=C4)O)N
Properties
Chemical formula	C40H50N8O10
Molar mass	802.886 g·mol−1
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa). N verify (what is YN ?) Infobox references

Dermorphin is not found in humans or other mammals and similar D-amino acid peptides have only been found in bacteria, amphibians, and molluscs.^[5] Dermorphin appears to be made in these through an unusual posttranslational modification carried out by an amino acid isomerase.^[6] This unusual process is needed because the D-alanine in this peptide is not among the 20 amino acids coded for in the genetic code and thus the peptide cannot be synthesized in the usual way from the encodings in the genome of an organism.

Illicit use

Dermorphin has been illegally used in horse racing as a performance-enhancing drug. Due to dermorphin's painkilling activity, horses treated with dermorphin may run harder than they would otherwise.^[7]

See also

• Deltorphin
• Deltorphin I