Characterization of drug interactions with serum proteins by using high-performance affinity chromatography

David S Hage, Jeanethe Anguizola, Omar Barnaby, Abby Jackson, Michelle J. Yoo, Efthimia Papastavros, Erika Pfaunmiller, Matt Sobansky, Zenghan Tong

Research output: Contribution to journalArticle

51 Citations (Scopus)

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, ai-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.

Original languageEnglish (US)
Pages (from-to)313-328
Number of pages16
JournalCurrent Drug Metabolism
Volume12
Issue number4
StatePublished - May 1 2011

Fingerprint

Drug interactions
Affinity chromatography
Drug Interactions
Affinity Chromatography
Blood Proteins
Pharmaceutical Preparations
Protein Binding
High-Throughput Screening Assays
Precision Medicine
Serum Albumin
Lipoproteins
Medicine
Toxicity
Glycoproteins
Screening
Binding Sites
Throughput
Acids
Serum

Keywords

  • Drug-protein binding
  • High-performance affinity chromatography
  • High-throughput screening
  • Human serum albumin
  • Lipoproteins
  • Personalized medicine
  • α-acid glycoprotein

ASJC Scopus subject areas

  • Pharmacology
  • Clinical Biochemistry

Cite this

Hage, D. S., Anguizola, J., Barnaby, O., Jackson, A., Yoo, M. J., Papastavros, E., ... Tong, Z. (2011). Characterization of drug interactions with serum proteins by using high-performance affinity chromatography. Current Drug Metabolism, 12(4), 313-328.

Characterization of drug interactions with serum proteins by using high-performance affinity chromatography. / Hage, David S; Anguizola, Jeanethe; Barnaby, Omar; Jackson, Abby; Yoo, Michelle J.; Papastavros, Efthimia; Pfaunmiller, Erika; Sobansky, Matt; Tong, Zenghan.

In: Current Drug Metabolism, Vol. 12, No. 4, 01.05.2011, p. 313-328.

Research output: Contribution to journalArticle

Hage, DS, Anguizola, J, Barnaby, O, Jackson, A, Yoo, MJ, Papastavros, E, Pfaunmiller, E, Sobansky, M & Tong, Z 2011, 'Characterization of drug interactions with serum proteins by using high-performance affinity chromatography', Current Drug Metabolism, vol. 12, no. 4, pp. 313-328.
Hage DS, Anguizola J, Barnaby O, Jackson A, Yoo MJ, Papastavros E et al. Characterization of drug interactions with serum proteins by using high-performance affinity chromatography. Current Drug Metabolism. 2011 May 1;12(4):313-328.
Hage, David S ; Anguizola, Jeanethe ; Barnaby, Omar ; Jackson, Abby ; Yoo, Michelle J. ; Papastavros, Efthimia ; Pfaunmiller, Erika ; Sobansky, Matt ; Tong, Zenghan. / Characterization of drug interactions with serum proteins by using high-performance affinity chromatography. In: Current Drug Metabolism. 2011 ; Vol. 12, No. 4. pp. 313-328.
@article{a1d3fbd4d52a4a5ca3a8d040cb0afcf4,
title = "Characterization of drug interactions with serum proteins by using high-performance affinity chromatography",
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, ai-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.",
keywords = "Drug-protein binding, High-performance affinity chromatography, High-throughput screening, Human serum albumin, Lipoproteins, Personalized medicine, α-acid glycoprotein",
author = "Hage, {David S} and Jeanethe Anguizola and Omar Barnaby and Abby Jackson and Yoo, {Michelle J.} and Efthimia Papastavros and Erika Pfaunmiller and Matt Sobansky and Zenghan Tong",
year = "2011",
month = "5",
day = "1",
language = "English (US)",
volume = "12",
pages = "313--328",
journal = "Current Drug Metabolism",
issn = "1389-2002",
publisher = "Bentham Science Publishers B.V.",
number = "4",

}

TY - JOUR

T1 - Characterization of drug interactions with serum proteins by using high-performance affinity chromatography

AU - Hage, David S

AU - Anguizola, Jeanethe

AU - Barnaby, Omar

AU - Jackson, Abby

AU - Yoo, Michelle J.

AU - Papastavros, Efthimia

AU - Pfaunmiller, Erika

AU - Sobansky, Matt

AU - Tong, Zenghan

PY - 2011/5/1

Y1 - 2011/5/1

N2 - 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, ai-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.

AB - 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, ai-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.

KW - Drug-protein binding

KW - High-performance affinity chromatography

KW - High-throughput screening

KW - Human serum albumin

KW - Lipoproteins

KW - Personalized medicine

KW - α-acid glycoprotein

UR - http://www.scopus.com/inward/record.url?scp=79953665313&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=79953665313&partnerID=8YFLogxK

M3 - Article

VL - 12

SP - 313

EP - 328

JO - Current Drug Metabolism

JF - Current Drug Metabolism

SN - 1389-2002

IS - 4

ER -