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Tritiated deltorphin analogues with high specific radioactivity and high affinity and selectivity for delta opioid receptors
Author(s) -
Darula Zsuzsa,
Péter Antal,
Tóth Géza
Publication year - 1997
Publication title -
journal of labelled compounds and radiopharmaceuticals
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.432
H-Index - 47
eISSN - 1099-1344
pISSN - 0362-4803
DOI - 10.1002/(sici)1099-1344(199710)39:10<817::aid-jlcr28>3.0.co;2-b
Subject(s) - chemistry , selectivity , potency , receptor , stereochemistry , tritium , amino acid , opioid , peptide , chemical synthesis , δ opioid receptor , catalysis , biochemistry , in vitro , physics , nuclear physics
New conformationally constrained deltorphin I and II analogues were designed and synthesized, using a more lipophilic amino acid (Ile) instead of Val at positions 5 and 6, and 2‐aminotetralin‐2‐carboxylic acid (Atc) at position 3. Two analogues (Tyr‐ D ‐Ala‐( S )‐Atc‐Asp‐Ile‐Ile‐Gly‐NH 2 and Tyr‐ D ‐Ala‐( R )‐Atc‐Glu‐Ile‐Ile‐Gly‐NH 2 ) with high potency and selectivity for δ opioid receptors were chosen for tritiation, with 3,5‐I 2 ‐Tyr 1 ‐deltorphin analogues as precursors. Catalytic dehalotritiation of these precursors resulted in tritiated peptides with high specific radioactivity (1.28 TBq/mmol (34.5 Ci/mmol) and 1.33 TBq/mmol (36.0 Ci/mmol), respectively). © 1997 John Wiley & Sons, Ltd.