Analysis of lidocaine interactions with serum proteins using high-performance affinity chromatography

Sony Soman, Michelle J. Yoo, Yoon Jeong Jang, David S. Hage

Research output: Contribution to journalArticlepeer-review

29 Scopus citations


High-performance affinity chromatography was used to study binding by the drug lidocaine to human serum albumin (HSA) and α1-acid glycoprotein (AGP). AGP had strong binding to lidocaine, with an association equilibrium constant (Ka) of 1.1-1.7 × 105 M-1 at 37 °C and pH 7.4. Lidocaine had weak to moderate binding to HSA, with a Ka in the range of 103 to 104 M-1. Competitive experiments with site selective probes showed that lidocaine was interacting with Sudlow site II of HSA and the propranolol site of AGP. These results agree with previous observations in the literature and provide a better quantitative understanding of how lidocaine binds to these serum proteins and is transported in the circulation. This study also demonstrates how HPAC can be used to examine the binding of a drug with multiple serum proteins and provide detailed information on the interaction sites and equilibrium constants that are involved in such processes.

Original languageEnglish (US)
Pages (from-to)705-708
Number of pages4
JournalJournal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences
Issue number7-8
StatePublished - Mar 1 2010


  • High-performance affinity chromatography
  • Human serum albumin
  • Lidocaine
  • α-Acid glycoprotein

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry
  • Clinical Biochemistry
  • Cell Biology


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