BW373U86, its enantiomers, and related compounds: Interactions of non-peptide delta agonists at multiple δcx binding sites in rat brain

X. Y. Cha, H. Xu, S. N. Calderon, L. E. Smith, K. C. Rice, F. Porreca, R. B. Rothman

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2 Scopus citations


Previous studies delineated two classes of δ binding sites: a δ binding site not associated with the opioid receptor complex, termed the δncx site, and a δ site associated with the opioid receptor complex, termed the δcx site (for review see (1)). More recent studies resolved two δcx binding sites in rat brain termed δcx-1 and δcx-2 (2). Pretreatment of membranes with the δ-selective acylating agent (+)-trans-SUPERFIT depletes membranes of the δncx binding site which permits selective labeling of the δcx binding sites with [3H]DADLE (3). Ligand-selectivity studies of the non-peptide δ agonist, BW373U86, its enantiomers and related compounds showed that these drugs have higher affinities for δ sites than μ sites (4,5). This study determined the selectivity of these compounds for the two δcx binding sites. The data indicate that (+)-4-[(αR)-α((2S,5R)-4-allyl-2,5-dimethyl-1- piperazinyl)-3-methoxybenzyl]-N,N-diethylbenzamide (SNC80) and deltorphin-II are highly selective for δcx-2 binding site (2758-fold and 700-fold respectively). In contrast, morphine is selective for δcx-1 binding site (78-fold).

Original languageEnglish (US)
Pages (from-to)45-46
Number of pages2
JournalRegulatory Peptides
Issue number1
StatePublished - Nov 10 1994


ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Endocrinology
  • Clinical Biochemistry
  • Cellular and Molecular Neuroscience

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