Specific ligand binding on genetic variants of human α 1-acid glycoprotein studied by circular dichroism spectroscopy

Research output: Contribution to journalArticle

37 Citations (Scopus)


Human α1-acid glycoprotein displays genetic polymorphism. Different drug binding properties of the two main genetic products (F1-S and A variants) have been demonstrated. In search for specific circular dichroism (CD) probes, dicumarol and acridine orange were found to specifically bind to the F1-S and A variants, respectively. Dicumarol binding to the F1-S variant produced induced Cotton effects originating from the favored chiral conformation of the bound label. Acridine orange gave induced biphasic Cotton effects due to chiral intermolecular exciton interaction between label molecules bound to the A variant. Displacement of the CD probes by specific marker ligands was demonstrated. The induced CD spectrum of dicumarol was found to change sign in the presence of imipramine, as a manifestation of high-affinity ternary complex formation on the F1-S variant.

Original languageEnglish
Pages (from-to)679-688
Number of pages10
JournalBiochemical Pharmacology
Issue number4
Publication statusPublished - Feb 15 2004


  • Acridine orange
  • Dicumarol
  • Genetic variants
  • Imipramine
  • Induced circular dichroism
  • α-Acid glycoprotein

ASJC Scopus subject areas

  • Biochemistry
  • Pharmacology

Fingerprint Dive into the research topics of 'Specific ligand binding on genetic variants of human α <sub>1</sub>-acid glycoprotein studied by circular dichroism spectroscopy'. Together they form a unique fingerprint.

  • Cite this