title: High-Performance Affinity Chromatography: Applications in Drug-Protein Binding Studies and Personalized Medicine.
abstract: The binding of drugs with proteins and other agents in serum is of interest in personalized medicine because this process can affect the dosage and action of drugs. The extent of this binding may also vary with a given disease state. These interactions may involve serum proteins, such as human serum albumin or α1-acid glycoprotein, or other agents, such as lipoproteins. High-performance affinity chromatography (HPAC) is a tool that has received increasing interest as a means for studying these interactions. This review discusses the general principles of HPAC and the various approaches that have been used in this technique to examine drug-protein binding and in work related to personalized medicine. These approaches include frontal analysis and zonal elution, as well as peak decay analysis, ultrafast affinity extraction, and chromatographic immunoassays. The operation of each method is described and examples of applications for these techniques are provided. The type of information that can be obtained by these methods is also discussed, as related to the analysis of drug-protein binding and the study of clinical or pharmaceutical samples.
authors.affiliation: Department of Chemistry, University of Nebraska-Lincoln, Lincoln, Nebraska, USA.
authors.forename: Zhao
authors.initials: Z
authors.lastname: Li
authors.affiliation: Department of Chemistry, University of Nebraska-Lincoln, Lincoln, Nebraska, USA.
authors.forename: Sandya R
authors.initials: SR
authors.lastname: Beeram
authors.affiliation: Department of Chemistry, University of Nebraska-Lincoln, Lincoln, Nebraska, USA.
authors.forename: Cong
authors.initials: C
authors.lastname: Bi
authors.affiliation: Department of Chemistry, University of Nebraska-Lincoln, Lincoln, Nebraska, USA.
authors.forename: D
authors.initials: D
authors.lastname: Suresh
authors.affiliation: Department of Chemistry, University of Nebraska-Lincoln, Lincoln, Nebraska, USA.
authors.forename: Xiwei
authors.initials: X
authors.lastname: Zheng
authors.affiliation: Department of Chemistry, University of Nebraska-Lincoln, Lincoln, Nebraska, USA. Electronic address: dhage1@unl.edu.
authors.forename: David S
authors.initials: DS
authors.lastname: Hage
mesh_terms: D001798:Blood Proteins / Q000737:chemistry / Q000378:metabolism*; D002846:Chromatography, Affinity / Q000379:methods*; D006801:Humans; D004364:Pharmaceutical Preparations / Q000737:chemistry* / Q000378:metabolism; D057285:Precision Medicine; D011485:Protein Binding
chemical_list: D001798:Blood Proteins; D004364:Pharmaceutical Preparations
keywords: Alpha(1)-acid glycoprotein; Drug–protein binding; Glycation; High-performance affinity chromatography; Human serum albumin; Lipoproteins; Personalized medicine