Binding characteristics of the novel highly selective delta agonist, [3H]Ile5,6deltorphin II

S. T. Nevin, L. Kabasakal, F. Ötvös, G. Töth, A. Borsodi

Research output: Article

65 Citations (Scopus)

Abstract

Following the description of the [3H]deltorphin II, it has been reported that the modification of deltorphin II with the substitution of Val5,6 residues by the more hydrophobic lle5,6 residues leads to an increased affinity and selectivity. The lle5,6deltorphin II (Tyr-D-Ala-Phe-Gly-lle-lle-Gly-NH2) was tritiated by catalytic dehalogenation and labelled rat brain membrane sites with a Kd value of 0.40 nM and a Bmax of 121 fmol/mg protein. Competition binding experiments with various unlabelled subtype specific opioid receptor ligands resulted in μ δ and κ δ selectivity ratios of 2400 and 18 000 respectively. Due to its high δ receptor affinity, δ selectivity and very low non-specific binding (3H]lle5,6deltorphin II, is a very useful tool for the identification and characterisation of δ opioid receptors.

Original languageEnglish
Pages (from-to)261-265
Number of pages5
JournalNeuropeptides
Volume26
Issue number4
DOIs
Publication statusPublished - 1994

Fingerprint

Opioid Receptors
Dehalogenation
Rats
Brain
Substitution reactions
Ligands
Membranes
Proteins
Experiments
Ala(2)-deltorphin II
tyrosyl-alanyl-glycyl-phenylalanine

ASJC Scopus subject areas

  • Biochemistry
  • Endocrinology
  • Endocrinology, Diabetes and Metabolism
  • Clinical Neurology
  • Neuroscience(all)
  • Cellular and Molecular Neuroscience

Cite this

Binding characteristics of the novel highly selective delta agonist, [3H]Ile5,6deltorphin II. / Nevin, S. T.; Kabasakal, L.; Ötvös, F.; Töth, G.; Borsodi, A.

In: Neuropeptides, Vol. 26, No. 4, 1994, p. 261-265.

Research output: Article

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AU - Borsodi, A.

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