Interaction of [D-Ser2,Leu5]enkephalin-Thr6 (DSLET), a relatively selective delta ligand, with MU1 opioid binding sites

Yossef Itzhak, Gavril W. Pasternak

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

Using binding approaches, we have confirmed the high selectivity of [D-Ser2,Leu5]enkephalin-Thr6 (DSLET) to delta, as opposed to morphine-preferring (mu2) sites in rat brain. However, detailed experiments studies indicate that this ligand also labels mu1 sites with very high affinity. Saturation studies of 3H-DSLET binding reveal curvilinear plots. Treating tissue with naloxonazine to block mu1 sites, eliminates the higher affinity binding component. Competition studies of the other peptites against 3H-DSLET and 3H[D-Ala2, MePhe4,Gly(ol)5] enkephalin (3H-DAMPGO) binding also implied high affinity binding of these peptides to mu1 sites. The ability of these peptides to interact with mu1 sites may help explain some of their pharmacological actions.

Original languageEnglish
Pages (from-to)307-311
Number of pages5
JournalLife Sciences
Volume40
Issue number3
DOIs
StatePublished - Jan 19 1987
Externally publishedYes

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Enkephalins
Opioid Analgesics
Binding Sites
Ligands
Peptides
Morphine
Rats
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Brain
Pharmacology
Tissue
Experiments

ASJC Scopus subject areas

  • Pharmacology

Cite this

Interaction of [D-Ser2,Leu5]enkephalin-Thr6 (DSLET), a relatively selective delta ligand, with MU1 opioid binding sites. / Itzhak, Yossef; Pasternak, Gavril W.

In: Life Sciences, Vol. 40, No. 3, 19.01.1987, p. 307-311.

Research output: Contribution to journalArticle

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