Synthesis and binding characteristics of the highly selective radiolabelled deltorphin analogues containing 2-aminotetralin-2-carboxylic acid in position 3

M. Spetea, Z. Darula, G. Tóth, A. Borsodi

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3 Citations (Scopus)

Abstract

Following the description of (3H]Ile5,6,deltorphin II, when it was reported that changes in hydrophobicity at positions 5 and 6 give rise to analogues with increased δ-receptor affinity and selectivity, new conformationally restricted deltorphin analogues were designed. A synthetic amino acid, 2-aminotetralin-2-carboxylic acid (Atc), was introduced at position 3 instead of Phe in IIe5,6deltorphin I and II, and the resultant compounds were prepared in tritiated form. Opioid binding sites specific for [3H]s-Atc3,Ile5,6deltorphin I and [3H]R-Atc3,Ile5,6deltorphin II were characterized in rat brain membranes. Their binding was saturable, stereoselective and inhibited by δ-selective ligands with high potency. They labelled single class of opioid sites at 35°C with high affinity (K(d) - 0.3 nM), B(max) values of 130 fmo/mg protein, and vary low non-specific binding was observed. Both tritiated deltorphin analogues showed δ-receptor specificity in rat brain, therefore they could represent excellent new radioligands for investigating the complexity of the opioid receptor systems.

Original languageEnglish
Pages (from-to)483-488
Number of pages6
JournalNeuropeptides
Volume31
Issue number5
Publication statusPublished - 1997

Fingerprint

Opioid Analgesics
Rats
Brain
Opioid Receptors
Hydrophobicity
Hydrophobic and Hydrophilic Interactions
Binding Sites
Ligands
Membranes
Amino Acids
Proteins
deltorphin
2-aminotetralin-2-carboxylic acid
Ala(2)-deltorphin II

ASJC Scopus subject areas

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

Cite this

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abstract = "Following the description of (3H]Ile5,6,deltorphin II, when it was reported that changes in hydrophobicity at positions 5 and 6 give rise to analogues with increased δ-receptor affinity and selectivity, new conformationally restricted deltorphin analogues were designed. A synthetic amino acid, 2-aminotetralin-2-carboxylic acid (Atc), was introduced at position 3 instead of Phe in IIe5,6deltorphin I and II, and the resultant compounds were prepared in tritiated form. Opioid binding sites specific for [3H]s-Atc3,Ile5,6deltorphin I and [3H]R-Atc3,Ile5,6deltorphin II were characterized in rat brain membranes. Their binding was saturable, stereoselective and inhibited by δ-selective ligands with high potency. They labelled single class of opioid sites at 35°C with high affinity (K(d) - 0.3 nM), B(max) values of 130 fmo/mg protein, and vary low non-specific binding was observed. Both tritiated deltorphin analogues showed δ-receptor specificity in rat brain, therefore they could represent excellent new radioligands for investigating the complexity of the opioid receptor systems.",
author = "M. Spetea and Z. Darula and G. T{\'o}th and A. Borsodi",
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AU - Spetea, M.

AU - Darula, Z.

AU - Tóth, G.

AU - Borsodi, A.

PY - 1997

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