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. 1989 Jul;86(13):5188-92.
doi: 10.1073/pnas.86.13.5188.

Deltorphins: a family of naturally occurring peptides with high affinity and selectivity for delta opioid binding sites

V Erspamer  1 , P Melchiorri, G Falconieri-Erspamer, L Negri, R Corsi, C Severini, D Barra, M Simmaco, G Kreil
Affiliations

Deltorphins: a family of naturally occurring peptides with high affinity and selectivity for delta opioid binding sites

V Erspamer et al. Proc Natl Acad Sci U S A. 1989 Jul.

Abstract

Deltorphins are endogenous linear heptapeptides, isolated from skin extracts of frogs belonging to the genus Phyllomedusa, that have a higher affinity and selectivity for delta opioid binding sites than any other natural compound known. Two deltorphins with the sequence Tyr-Ala-Phe-Asp(or Glu)-Val-Val-Gly-NH2 have been isolated from skin extracts of Phyllomedusa bicolor. The alanine in position 2 is in the D configuration. These peptides, [D-Ala2]deltorphins I and II, show an even higher affinity for delta receptors than the previously characterized deltorphin, which contains D-methionine as the second amino acid. These peptides show some similarity to another constituent of Phyllomedusa skin, dermorphin, which is highly selective for mu-opioid receptors. These peptides all have the N-terminal sequence Tyr-D-Xaa-Phe, where D-Xaa is either D-alanine or D-methionine. While this structure seems to be capable of activating both mu and delta opioid receptors, differences in the C-terminal regions of these peptides are probably responsible for the observed high receptor selectivity of dermorphin and deltorphin.

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