[125I-Tyr1]biphalin binding to opioid receptors of rat brain and NG108-15 cell membranes

Jirina Slaninova, Suzanne M. Appleyard, Aleksandra Misicka, Andrzej W. Lipkowski, Richard J. Knapp, Steven J. Weber, Thomas P. Davis, Henry I. Yamamura, Victor J. Hruby

Research output: Contribution to journalArticlepeer-review

17 Scopus citations


Mono iodinated analogues of biphalin [(Tyr-D-Ala-Gly-Phe-NH-)2], both nonradioactive [I-Tyr1]biphalin and radioactive [125-Tyr1]biphalin have been synthesized. The radioligand binding profiles of these compounds for two types of tissues, rat brain membranes, and NG108-15 cell membranes were identical to the parent biphalin. This is additional evidence for the hypothesis that biphalin behaves like a monomeric ligand and that only one intact tyrosine is necessary for high biological activity. The second tyrosine could be used for successful radioiodination which may greatly simplify biochemical and pharmacological studies of biphalin. The results of receptor binding studies show that the binding of both biphalin and [I- Tyr1]biphalin to the δ and μ opioid receptors are not independent. [125I-Tyr1]Biphalin binds to δ receptors as shown in NG108-15 cell membranes. Nevertheless, [125I]biphalin binding to δ receptors in rat brain membranes was hardly evident and μ receptor binding predominated or at least was much more readily detectable in this preparation.

Original languageEnglish (US)
Pages (from-to)PL199-PL204
JournalLife Sciences
Issue number14
StatePublished - Feb 27 1998


  • Biphalin
  • Opioid peptides
  • [I-Tyr]biphalin
  • δ opioid receptors
  • μ opioid receptors

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Pharmacology, Toxicology and Pharmaceutics(all)


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