Biointeraction analysis of carbamazepine binding to α 1- acid glycoprotein by high-performance affinity chromatography

Hai Xuan, K. S. Joseph, Chunling Wa, David S. Hage

Research output: Contribution to journalArticle

25 Scopus citations

Abstract

Interactions of the drug carbamazepine with the serum protein α 1-acid glycoprotein (AGP) were examined by high-performance affinity chromatography. Frontal analysis studies with an immobilized AGP column and control column indicated carbamazepine had both low-affinity interactions with the support and high-affinity interactions with AGP. When a correction was made for binding to the support, the association equilibrium constant measured at pH 7.4 and 37°C for carbamazepine with AGP was 1.0 (±0.1) × 10 5 M -1, with values that ranged from 5.1 to 0.58 × 10 5 M -1 in going from 5 to 45°C. It was found in competition studies that these interactions were occurring at the same site that binds propranolol on AGP. Temperature studies indicated that the change in enthalpy was the main driving force for the binding of carbamazepine to AGP. These results provide a more complete picture of how carbamazepine binds to AGP in serum. This report also illustrates how high-performance affinity chromatography can be used to examine biological interactions and drug-protein binding in situations in which significant interactions for an analyte are present with both the chromatographic support and an immobilized ligand.

Original languageEnglish (US)
Pages (from-to)2294-2301
Number of pages8
JournalJournal of Separation Science
Volume33
Issue number15
DOIs
StatePublished - Aug 1 2010

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Keywords

  • Biointeraction analysis
  • Carbamazepine
  • Drug-protein binding
  • High-performance affinity chromatography
  • α -acid glycoprotein

ASJC Scopus subject areas

  • Analytical Chemistry
  • Filtration and Separation

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