Dermorphin

{{Short description|Opioid agonist peptide compound}}

{{cs1 config|name-list-style=vanc}}

{{chembox

| Verifiedfields = changed

| Watchedfields = changed

| verifiedrevid = 413081297

| ImageFile=dermorphin.svg

| ImageSize=300px

| ImageAlt=Skeletal formula of dermorphin

| ImageFile1=Dermorphin 3D spacefill.png

| ImageSize1=300

| ImageAlt1=Space-filling model of the dermorphin molecule

| IUPACName=

| OtherNames=Tyrosyl-alanyl-phenylalanyl-glycyl-tyrosyl-prolyl-serinamide

|Section1={{Chembox Identifiers

| CASNo_Ref = {{cascite|correct|??}}

| CASNo=77614-16-5

| UNII_Ref = {{fdacite|correct|FDA}}

| UNII = 2SEC01B703

| PubChem=5485199

| ChEMBL_Ref = {{ebicite|changed|EBI}}

| ChEMBL = 278789

| 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

| ChemSpiderID_Ref = {{chemspidercite|changed|chemspider}}

| ChemSpiderID = 4588650

| 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

| InChIKey = FHZPGIUBXYVUOY-VWGYHWLBBR

| StdInChI_Ref = {{stdinchicite|changed|chemspider}}

| StdInChI = 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

| StdInChIKey_Ref = {{stdinchicite|changed|chemspider}}

| StdInChIKey = FHZPGIUBXYVUOY-VWGYHWLBSA-N

}}

|Section2={{Chembox Properties

| C=40 | H=50 | N=8 | O=10

| Appearance=

| Density=

| MeltingPt=

| BoilingPt=

| Solubility=

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|Section3={{Chembox Hazards

| MainHazards=

| FlashPt=

| AutoignitionPt =

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Dermorphin is a hepta-peptide first isolated from the skin of South American frogs belonging to the genus Phyllomedusa.{{cite journal |vauthors=Melchiorri P, Negri L |title=The dermorphin peptide family |journal=Gen. Pharmacol. |volume=27 |issue=7 |pages=1099–107 |year=1996 |pmid=8981054 |doi=10.1016/0306-3623(95)02149-3}} The peptide is a natural opioid that binds as an agonist with high potency and selectivity to mu opioid receptors.{{cite book |vauthors=Amiche M, Delfour A, Nicolas P |chapter=Opioid peptides from frog skin |title=D-Amino Acids in Sequences of Secreted Peptides of Multicellular Organisms |journal=Exs |volume=85 |pages=57–71 |year=1998 |pmid=9949868 |doi=10.1007/978-3-0348-8837-0_4|doi-broken-date=1 November 2024 |isbn=978-3-0348-9794-5 }}{{cite journal |vauthors=Erspamer V, Melchiorri P, Falconieri-Erspamer G |title=Deltorphins: a family of naturally occurring peptides with high affinity and selectivity for delta opioid binding sites |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue=13 |pages=5188–92 |year=1989 |pmid=2544892 |doi=10.1073/pnas.86.13.5188 |pmc=297583|bibcode=1989PNAS...86.5188E |display-authors=etal|doi-access=free }} Dermorphin is about 30–40 times more potent than morphine, but theoretically may be less likely to produce drug tolerance and addiction due to its high potency.{{cite journal |vauthors=Broccardo M, Erspamer V, Falconieri Erspamer G |title=Pharmacological data on dermorphins, a new class of potent opioid peptides from amphibian skin |journal=Br. J. Pharmacol. |volume=73 |issue=3 |pages=625–31 |year=1981 |pmid=7195758 |pmc=2071698 |doi=10.1111/j.1476-5381.1981.tb16797.x|display-authors=etal}} The amino acid sequence of dermorphin is H-Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH₂.

Dermorphin is not found in humans or other mammals and similar D-amino acid peptides have only been found in bacteria, amphibians, and molluscs.{{cite journal |author=Kreil G |title=Peptides containing a D-amino acid from frogs and molluscs |journal=J. Biol. Chem. |volume=269 |issue=15 |pages=10967–70 |date=15 April 1994|doi=10.1016/S0021-9258(19)78075-2 |pmid=8157620 |url=http://www.jbc.org/cgi/reprint/269/15/10967 |doi-access=free }} Dermorphin appears to be made in these through an unusual posttranslational modification carried out by an amino acid isomerase.{{cite journal |vauthors=Heck SD, Faraci WS, Kelbaugh PR, Saccomano NA, Thadeio PF, Volkmann RA |title=Posttranslational amino acid epimerization: enzyme-catalyzed isomerization of amino acid residues in peptide chains |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue=9 |pages=4036–9 |year=1996 |pmid=8633012 |doi=10.1073/pnas.93.9.4036 |pmc=39482|bibcode=1996PNAS...93.4036H |doi-access=free }} 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.