Interactions of the carrier ligands of antidiabetic metal complexes with human serum albumin: A combined spectroscopic and separation approach with molecular modeling studies

Éva A. Enyedy, László Horváth, Anasztázia Hetényi, Tiziano Tuccinardi, Christian G. Hartinger, Bernhard K. Keppler, Tamás Kiss

Research output: Contribution to journalArticle

17 Citations (Scopus)


The specific binding of carrier ligands of antidiabetic vanadium(IV) and zinc(II) complexes into drug binding pockets of human serum albumin (HSA) has been investigated via displacement reactions of site markers such as warfarin and dansylglycine by different spectroscopic (fluorescence, circular dichroism, NMR) and separation methods (capillary zone electrophoresis, ultrafiltration-UV). Conditional stability constants of the ligands were calculated for the binding at sites I and II of HSA. Binding site I was found to be the primary binding site for 2,6-pyridine dicarboxylic acid (dipic) and picolinic acid (pic), and site II for 6-methylpicolinic acid (6-Mepic) and maltol, although dipic, 6-Mepic and pic displace both site markers at differing extents. The experimental data is complemented by protein-ligand docking calculations for dipic and 6-Mepic which support the observations.

Original languageEnglish
Pages (from-to)4202-4210
Number of pages9
JournalBioorganic and Medicinal Chemistry
Issue number14
Publication statusPublished - Jul 15 2011



  • Fluorimetry
  • Protein-ligand interaction
  • Site markers
  • Solution equilibrium
  • Stability constants

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmaceutical Science
  • Drug Discovery
  • Clinical Biochemistry
  • Organic Chemistry

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