The Determination of Drug Protein Binding by HPLC Using a Chemically Bonded Bovine-Albumin Stationary Phase

  • N. Lammers
  • H. de Bree
  • C. P. Groen
  • H. M. Ruijten
  • B. J. de Jong
Part of the Methodological Surveys in Biochemistry and Analysis book series (MSBA, volume 18 A)

Abstract

The binding of drugs to proteins may play an important role in drug bioavailability and in interactions with other drugs bound to proteins. Determination of drug protein binding by equilibrium dialysis [1] is rather time-consuming; size-exclusion chromatography has been described as an alternative [2], but special precautions are required to prevent dissociation of the drug-protein comples [3]. Yoshida et al. [4] used proteins physically bonded to ODS (C-18) columns to separate drugs. Here we describe the use of a commercially available chemically bonded bovine-albumin stationary phase to determine the degree of protein binding of potential drugs. To obtain the required hydrophobic interaction a buffer concentration of ~0.1 M is necessary, and the addition of 1-propanol lowers retention for all solutes [5]. The retention characteristics of a heterogeneous group of 23 compounds and a group of 11 analogous potential drugs has now been studied. We compared the resulting data with equilibrium dialysis results. The amount injected for chromatography had to be small (~0.5 pmol) to prevent overloading of the Chromatographic system.

Keywords

Sulfa Compound Potential Drug Buffer Concentration retentIon Volume Equilibrium Dialysis 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1988

Authors and Affiliations

  • N. Lammers
    • 1
  • H. de Bree
    • 1
  • C. P. Groen
    • 1
  • H. M. Ruijten
    • 1
  • B. J. de Jong
    • 1
  1. 1.Analytical Development DepartmentDuphar Research LaboratoriesWeespThe Netherlands

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