Characterization of Drug Interactions with Serum Proteins by Using High-performance Affinity Chromatography

Overview

Journal Curr Drug Metab

Publisher Bentham Science Publishers

Specialties Chemistry
Endocrinology

Date 2011 Mar 15

PMID 21395530

Citations 28

Authors

David S Hage

Jeanethe Anguizola

Omar Barnaby

Abby Jackson

Michelle J Yoo

Efthimia Papastavros

Erika Pfaunmiller

Matt Sobansky

Zenghan Tong

Affiliations

Soon will be listed here.

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, α(1)-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.

Citing Articles

Binding studies of promethazine and its metabolites with human serum albumin by high-performance affinity chromatography and molecular docking in the presence of codeine.

Coelho M, Lima R, Almeida A, Fernandes P, Remiao F, Fernandes C Anal Bioanal Chem. 2024; 416(20):4605-4618.

PMID: 38965103 PMC: 11294390. DOI: 10.1007/s00216-024-05409-3.

Turning adversity into opportunity: Small extracellular vesicles as nanocarriers for tumor-associated macrophages re-education.

Donoso-Meneses D, Figueroa-Valdes A, Georges N, Tobar H, Alcayaga-Miranda F Bioeng Transl Med. 2023; 8(1):e10349.

PMID: 36684102 PMC: 9842057. DOI: 10.1002/btm2.10349.

Studies of binding by sulfonylureas with glyoxal- and methylglyoxal-modified albumin by immunoextraction using affinity microcolumns.

Rodriguez E, Tao P, Woolfork A, Li Z, Matsuda R, Sun Z J Chromatogr A. 2020; 1638:461683.

PMID: 33223150 PMC: 7870548. DOI: 10.1016/j.chroma.2020.461683.

Characterization of solution-phase drug-protein interactions by ultrafast affinity extraction.

Beeram S, Zheng X, Suh K, Hage D Methods. 2018; 146:46-57.

PMID: 29510250 PMC: 6098730. DOI: 10.1016/j.ymeth.2018.02.021.

Analysis of solute-protein interactions and solute-solute competition by zonal elution affinity chromatography.

Tao P, Poddar S, Sun Z, Hage D, Chen J Methods. 2018; 146:3-11.

PMID: 29409783 PMC: 6072616. DOI: 10.1016/j.ymeth.2018.01.020.

References

Kim H, Hage D . Chromatographic analysis of carbamazepine binding to human serum albumin. J Chromatogr B Analyt Technol Biomed Life Sci. 2005; 816(1-2):57-66. DOI: 10.1016/j.jchromb.2004.11.006. View

Kremer J, Wilting J, Janssen L . Drug binding to human alpha-1-acid glycoprotein in health and disease. Pharmacol Rev. 1988; 40(1):1-47. View

Yoo M, Hage D . Use of peak decay analysis and affinity microcolumns containing silica monoliths for rapid determination of drug-protein dissociation rates. J Chromatogr A. 2010; 1218(15):2072-8. PMC: 3024456. DOI: 10.1016/j.chroma.2010.09.070. View

Mallik R, Xuan H, Guiochon G, Hage D . Immobilization of alpha1-acid glycoprotein for chromatographic studies of drug-protein binding II. correction for errors in association constant measurements. Anal Biochem. 2008; 376(1):154-6. PMC: 2386853. DOI: 10.1016/j.ab.2008.01.035. View

Hodgson R, Brook M, Brennan J . Capillary-scale monolithic immunoaffinity columns for immunoextraction with in-line laser-induced fluorescence detection. Anal Chem. 2005; 77(14):4404-12. DOI: 10.1021/ac048142p. View

Schiel J, Ohnmacht C, Hage D . Measurement of drug-protein dissociation rates by high-performance affinity chromatography and peak profiling. Anal Chem. 2009; 81(11):4320-33. PMC: 3443976. DOI: 10.1021/ac9000404. View

Busch M, Carels L, Boelens H, Kraak J, Poppe H . Comparison of five methods for the study of drug-protein binding in affinity capillary electrophoresis. J Chromatogr A. 1997; 777(2):311-28. DOI: 10.1016/s0021-9673(97)00369-5. View

Mallik R, Wa C, Hage D . Development of sulfhydryl-reactive silica for protein immobilization in high-performance affinity chromatography. Anal Chem. 2007; 79(4):1411-24. PMC: 2528201. DOI: 10.1021/ac061779j. View

Hage D, Tweed S . Recent advances in chromatographic and electrophoretic methods for the study of drug-protein interactions. J Chromatogr B Biomed Sci Appl. 1997; 699(1-2):499-525. DOI: 10.1016/s0378-4347(97)00178-3. View

10.

Beaudry F, Coutu M, Brown N . Determination of drug-plasma protein binding using human serum albumin chromatographic column and multiple linear regression model. Biomed Chromatogr. 1999; 13(6):401-6. DOI: 10.1002/(SICI)1099-0801(199910)13:6<401::AID-BMC899>3.0.CO;2-C. View

11.

Aubry A, Markoglou N, McGann A . Comparison of drug binding interactions on human, rat and rabbit serum albumin using high-performance displacement chromatography. Comp Biochem Physiol C Pharmacol Toxicol Endocrinol. 1995; 112(3):257-66. DOI: 10.1016/0742-8413(95)02019-5. View

12.

Loun B, Hage D . Chiral separation mechanisms in protein-based HPLC columns. 2. Kinetic studies of (R)- and (S)-warfarin binding to immobilized human serum albumin. Anal Chem. 1996; 68(7):1218-25. DOI: 10.1021/ac950827p. View

13.

Joseph K, Anguizola J, Hage D . Binding of tolbutamide to glycated human serum albumin. J Pharm Biomed Anal. 2010; 54(2):426-32. PMC: 2962718. DOI: 10.1016/j.jpba.2010.09.003. View

14.

Hage D, Noctor T, Wainer I . Characterization of the protein binding of chiral drugs by high-performance affinity chromatography. Interactions of R- and S-ibuprofen with human serum albumin. J Chromatogr A. 1995; 693(1):23-32. DOI: 10.1016/0021-9673(94)01009-4. View

15.

Nakano N, Shimamori Y, Yamaguchi S . Mutual displacement interactions in the binding of two drugs to human serum albumin by frontal affinity chromatography. J Chromatogr. 1980; 188(2):347-56. DOI: 10.1016/s0021-9673(00)81257-1. View

16.

Allenmark S . Chiral discrimination by albumin: a mechanistic study of liquid chromatographic optical resolution of nonaromatic carboxylic acids. Chirality. 1993; 5(5):295-9. DOI: 10.1002/chir.530050503. View

17.

Peyrin E, Guillaume Y, Guinchard C . Peculiarities of dansyl amino acid enantioselectivity using human serum albumin as a chiral selector. J Chromatogr Sci. 1998; 36(2):97-103. DOI: 10.1093/chromsci/36.2.97. View

18.

Chen J, Ohnmacht C, Hage D . Studies of phenytoin binding to human serum albumin by high-performance affinity chromatography. J Chromatogr B Analyt Technol Biomed Life Sci. 2004; 809(1):137-45. DOI: 10.1016/j.jchromb.2004.06.012. View

19.

Wasan K, Cassidy S . Role of plasma lipoproteins in modifying the biological activity of hydrophobic drugs. J Pharm Sci. 1998; 87(4):411-24. DOI: 10.1021/js970407a. View

20.

Gyimesi-Forras K, Szasz G, Gergely A, Szabo M, Kokosi J . Optical resolution of a series of potential cholecystokinin antagonist 4(3H)-quinazolone derivatives by chiral liquid chromatography on alpha1-acid glycoprotein stationary phase. J Chromatogr Sci. 2000; 38(10):430-4. DOI: 10.1093/chromsci/38.10.430. View