Characterization Of Drug Interactions With Serum Proteins by Using High-Performance Affinity Chromatography

Authors

David S. Hage, University of Nebraska-LincolnFollow
Jeanethe Anguizola, University of Nebraska-Lincoln
Omar S. Barnaby, University of Nebraska-LincolnFollow
Abby Jo Jackson, University of Nebraska - Lincoln
Michelle J. Yoo, University of Nebraska-Lincoln
Efthimia Papastavros, University of Nebraska-LincolnFollow
Erika Pfaunmiller, University of Nebraska-Lincoln
Matt Sobansky, University of Nebraska-Lincoln
Zenghan Tong, University of Nebraska-Lincoln

Date of this Version

5-2011

Citation

Published in final edited form as: Curr Drug Metab.2011 May ; 12(4): 313–328. Version presented here is from NIH PubMed Central.

Comments

Copyright Bentham Science. Used by permission.

Abstract

The binding of drugs with serum proteins can affect the activity, distribution, rate of excretion, and toxicity of pharmaceutical agents in the body. One tool that can be used to quickly analyze and characterize these interactions is high-performance affinity chromatography (HPAC). This review shows how HPAC can be used to study drug-protein binding and describes the various applications of this approach when examining drug interactions with serum proteins. Methods for determining binding constants, characterizing binding sites, examining drug-drug interactions, and studying drug-protein dissociation rates will be discussed. Applications that illustrate the use of HPAC with serum binding agents such as human serum albumin, α₁-acid glycoprotein, and lipoproteins will be presented. Recent developments will also be examined, such as new methods for immobilizing serum proteins in HPAC columns, the utilization of HPAC as a tool in personalized medicine, and HPAC methods for the high-throughput screening and characterization of drug-protein binding.