Species-dependency in chiral-drug recognition of serum albumin studied by chromatographic methods

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Stereoselective binding of benzodiazepine and coumarin drugs to serum albumin from human and six mammalian species were studied by chiral chromatographic techniques. The applied methods were affinity chromatography on the albumins immobilized on Sepharose 4B, high-performance liquid chromatography (HPLC) separation on columns based on human serum albumin (HSA) and bovine serum albumin (BSA), and chiral HPLC analysis of ultrafiltrates of solutions containing the racemic drug and the native protein. Substantial differences in preferred configurations and conformations were detected among the species. The binding stereoselectivity of the 2,3-benzodiazepine drug, tofisopam, in human, is opposite to that in all other species. In the binding of 1,4-benzodiazepines, dog albumin is very similar to HSA. Highly preferred binding of (S)-phenprocoumon was found with dog albumin.

Original languageEnglish
Pages (from-to)71-84
Number of pages14
JournalJournal of biochemical and biophysical methods
Issue number1-3
Publication statusPublished - Dec 31 2002


  • Affinity chromatography
  • Chiral separation
  • Immobilized protein
  • Stereoselective binding

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry

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