Dermorphin: Difference between revisions

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| ImageFile=dermorphin.svg
| ImageFile=dermorphin.svg
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| ImageAlt=Skeletal formula of dermorphin
| ImageAlt=Skeletal formula of dermorphin
| ImageFile1=Dermorphin 3D spacefill.png
| ImageFile1=Dermorphin 3D spacefill.png
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| ImageAlt1=Space-filling model of the dermorphin molecule
| ImageAlt1=Space-filling model of the dermorphin molecule
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'''Dermorphin''' is a hepta-[[peptide]] first isolated from the skin of South American [[frog]]s belonging to the genus ''[[Phyllomedusa]]''.<ref>{{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}}</ref> The peptide is a natural [[opioid]] that binds as an [[agonist]] with high potency and selectivity to [[mu opioid receptor]]s.<ref>{{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 }}</ref><ref>{{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 }}</ref> Dermorphin is about 30–40 times more potent than [[morphine]], but theoretically may be less likely to produce [[drug tolerance]] and [[Substance dependence|addiction]] due to its high potency.<ref>{{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}}</ref>  The amino acid sequence of dermorphin is H-Tyr-<small>D</small>-Ala-Phe-Gly-Tyr-Pro-Ser-NH<sub>2</sub>.
'''Dermorphin''' is a hepta-[[peptide]] first isolated from the skin of South American [[frog]]s belonging to the genus ''[[Phyllomedusa]]''.<ref>{{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}}</ref> The peptide is a natural [[opioid]] that binds as an [[agonist]] with high potency and selectivity to [[mu opioid receptor]]s.<ref>{{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=11 July 2025 |isbn=978-3-0348-9794-5 }}</ref><ref>{{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 }}</ref> Dermorphin is about 30–40 times more potent than [[morphine]].<ref>{{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}}</ref>  The amino acid sequence of dermorphin is H-Tyr-<small>D</small>-Ala-Phe-Gly-Tyr-Pro-Ser-NH<sub>2</sub>.


Dermorphin is not found in humans or other mammals and similar <small>D</small>-[[amino acid]] peptides have only been found in [[bacteria]], [[amphibian]]s, and [[molluscs]].<ref>{{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 }}</ref> Dermorphin appears to be made in these through an unusual [[posttranslational modification]] carried out by an amino acid isomerase.<ref>{{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 }}</ref> This unusual process is needed because the <small>D</small>-alanine in this peptide is not among the 20 amino acids coded for in the [[genetic code]] and thus the peptide cannot be [[Protein biosynthesis|synthesize]]d in the usual way from the encodings in the [[genome]] of an [[organism]].
Dermorphin is not found in humans or other mammals and similar [[D-Amino acid|D-amino acid]] peptides have only been found in [[bacteria]], [[amphibian]]s, and [[molluscs]].<ref>{{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 |doi-access=free }}</ref> Dermorphin appears to be made in these through an unusual [[posttranslational modification]] carried out by an amino acid [[isomerase]].<ref>{{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 }}</ref> This unusual process is needed because the <small>D</small>-alanine in this peptide is not among the 20 amino acids coded for in the [[genetic code]] and thus the peptide cannot be [[Protein biosynthesis|synthesize]]d in the usual way from the encodings in the [[genome]] of an [[organism]].


== Illicit use ==
== Illicit use ==
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* [[Deltorphin]]
* [[Deltorphin]]
* [[Deltorphin I]]
* [[Deltorphin I]]
* [[KGOP01]]


==References==
==References==

Latest revision as of 04:44, 24 December 2025

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Dermorphin
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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 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

References

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