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 opiate 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 but less likely to produce drug tolerance and addiction.[4]

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] The reason why such an unusual process is needed is because the D-alanine in this peptide is not among the 20 in the genetic code and cannot be encoded in the genes by higher organisms.

  • Structure of dermorphin: H-Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH2
  • Chemical formula: C40H50N8O10
  • Molecular weight: 802.9 g/mol

References

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External links

es:Dermorfina

ja:デルモルフィン

no:dermorfin
  1. Melchiorri P, Negri L (1996). "The dermorphin peptide family". Gen. Pharmacol. 27 (7): 1099–107. PMID 8981054. 
  2. Amiche M, Delfour A, Nicolas P (1998). "Opioid peptides from frog skin". EXS. 85: 57–71. PMID 9949868. 
  3. Erspamer V, Melchiorri P, Falconieri-Erspamer G; et al. (1989). "Deltorphins: a family of naturally occurring peptides with high affinity and selectivity for delta opioid binding sites". Proc. Natl. Acad. Sci. U.S.A. 86 (13): 5188–92. doi:10.1073/pnas.86.13.5188. PMC 297583Freely accessible. PMID 2544892. 
  4. Broccardo M, Erspamer V, Falconieri Erspamer G; et al. (1981). "Pharmacological data on dermorphins, a new class of potent opioid peptides from amphibian skin". Br. J. Pharmacol. 73 (3): 625–31. PMC 2071698Freely accessible. PMID 7195758. 
  5. Kreil G (15 April 1994). "Peptides containing a D-amino acid from frogs and molluscs". J. Biol. Chem. 269 (15): 10967–70. PMID 8157620. 
  6. Heck SD, Faraci WS, Kelbaugh PR, Saccomano NA, Thadeio PF, Volkmann RA (1996). "Posttranslational amino acid epimerization: enzyme-catalyzed isomerization of amino acid residues in peptide chains". Proc. Natl. Acad. Sci. U.S.A. 93 (9): 4036–9. doi:10.1073/pnas.93.9.4036. PMC 39482Freely accessible. PMID 8633012.