Studies of drug interactions with alpha1-acid glycoprotein by using on-line immunoextraction and high-performance affinity chromatography

Cong Bi, Ryan Matsuda, Chenhua Zhang, Zitha Isingizwe, William Clarke, David S. Hage

Research output: Contribution to journalArticle

Abstract

A method that combined on-line immunoextraction with high-performance affinity chromatography was developed to examine the binding of drugs with α1-acid glycoprotein (AGP). Affinity microcolumns containing immobilized polyclonal anti-AGP antibodies were developed that had a capture efficiency of up to 98.4% for AGP and a binding capacity of 0.72nmol AGP when using a 20mm×2.1mm i.d. microcolumn. These microcolumns were employed in various formats to examine the binding of drugs to normal AGP and AGP that had been adsorbed from serum samples for patients with systemic lupus erythematosus (SLE). Drugs that were screened in zonal elution experiments for their overall binding to these types of AGP included chlorpromazine, disopyramide, imipramine, propranolol, and warfarin. Most of these drugs showed an increase in their binding to the AGP from SLE serum when compared to normal AGP (i.e., an increase of 13-76%); however, disopyramide gave a 21-25% decrease in retention when the same AGP samples were compared. Frontal analysis was used to further evaluate the binding of disopyramide and imipramine to these forms of AGP. Both drugs gave a good fit to a model that involved a combination of saturable and non-saturable interactions with AGP. Changes in the non-saturable interactions accounted for most of variations seen in the binding of disopyramide and imipramine with the AGP samples. The methods used in this study could be adapted for use in personalized medicine and the study of other proteins or drugs using aqueous mixtures or clinical samples.

Original languageEnglish (US)
JournalJournal of Chromatography A
DOIs
StateAccepted/In press - 2017

Fingerprint

Drug interactions
Affinity chromatography
Drug Interactions
Affinity Chromatography
Glycoproteins
Acids
Disopyramide
Imipramine
Pharmaceutical Preparations
Systemic Lupus Erythematosus
Precision Medicine
Chlorpromazine
Warfarin
Serum
Propranolol

Keywords

  • Alpha-acid glycoprotein
  • Drug-protein interactions
  • High-performance affinity chromatography
  • Immunoextraction
  • Personalized medicine
  • Systemic lupus erythematosus

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry
  • Organic Chemistry

Cite this

Studies of drug interactions with alpha1-acid glycoprotein by using on-line immunoextraction and high-performance affinity chromatography. / Bi, Cong; Matsuda, Ryan; Zhang, Chenhua; Isingizwe, Zitha; Clarke, William; Hage, David S.

In: Journal of Chromatography A, 2017.

Research output: Contribution to journalArticle

@article{afef7207a2434e5486aa4ffa4b099ce1,
title = "Studies of drug interactions with alpha1-acid glycoprotein by using on-line immunoextraction and high-performance affinity chromatography",
abstract = "A method that combined on-line immunoextraction with high-performance affinity chromatography was developed to examine the binding of drugs with α1-acid glycoprotein (AGP). Affinity microcolumns containing immobilized polyclonal anti-AGP antibodies were developed that had a capture efficiency of up to 98.4{\%} for AGP and a binding capacity of 0.72nmol AGP when using a 20mm×2.1mm i.d. microcolumn. These microcolumns were employed in various formats to examine the binding of drugs to normal AGP and AGP that had been adsorbed from serum samples for patients with systemic lupus erythematosus (SLE). Drugs that were screened in zonal elution experiments for their overall binding to these types of AGP included chlorpromazine, disopyramide, imipramine, propranolol, and warfarin. Most of these drugs showed an increase in their binding to the AGP from SLE serum when compared to normal AGP (i.e., an increase of 13-76{\%}); however, disopyramide gave a 21-25{\%} decrease in retention when the same AGP samples were compared. Frontal analysis was used to further evaluate the binding of disopyramide and imipramine to these forms of AGP. Both drugs gave a good fit to a model that involved a combination of saturable and non-saturable interactions with AGP. Changes in the non-saturable interactions accounted for most of variations seen in the binding of disopyramide and imipramine with the AGP samples. The methods used in this study could be adapted for use in personalized medicine and the study of other proteins or drugs using aqueous mixtures or clinical samples.",
keywords = "Alpha-acid glycoprotein, Drug-protein interactions, High-performance affinity chromatography, Immunoextraction, Personalized medicine, Systemic lupus erythematosus",
author = "Cong Bi and Ryan Matsuda and Chenhua Zhang and Zitha Isingizwe and William Clarke and Hage, {David S.}",
year = "2017",
doi = "10.1016/j.chroma.2017.08.073",
language = "English (US)",
journal = "Journal of Chromatography",
issn = "0021-9673",
publisher = "Elsevier",

}

TY - JOUR

T1 - Studies of drug interactions with alpha1-acid glycoprotein by using on-line immunoextraction and high-performance affinity chromatography

AU - Bi, Cong

AU - Matsuda, Ryan

AU - Zhang, Chenhua

AU - Isingizwe, Zitha

AU - Clarke, William

AU - Hage, David S.

PY - 2017

Y1 - 2017

N2 - A method that combined on-line immunoextraction with high-performance affinity chromatography was developed to examine the binding of drugs with α1-acid glycoprotein (AGP). Affinity microcolumns containing immobilized polyclonal anti-AGP antibodies were developed that had a capture efficiency of up to 98.4% for AGP and a binding capacity of 0.72nmol AGP when using a 20mm×2.1mm i.d. microcolumn. These microcolumns were employed in various formats to examine the binding of drugs to normal AGP and AGP that had been adsorbed from serum samples for patients with systemic lupus erythematosus (SLE). Drugs that were screened in zonal elution experiments for their overall binding to these types of AGP included chlorpromazine, disopyramide, imipramine, propranolol, and warfarin. Most of these drugs showed an increase in their binding to the AGP from SLE serum when compared to normal AGP (i.e., an increase of 13-76%); however, disopyramide gave a 21-25% decrease in retention when the same AGP samples were compared. Frontal analysis was used to further evaluate the binding of disopyramide and imipramine to these forms of AGP. Both drugs gave a good fit to a model that involved a combination of saturable and non-saturable interactions with AGP. Changes in the non-saturable interactions accounted for most of variations seen in the binding of disopyramide and imipramine with the AGP samples. The methods used in this study could be adapted for use in personalized medicine and the study of other proteins or drugs using aqueous mixtures or clinical samples.

AB - A method that combined on-line immunoextraction with high-performance affinity chromatography was developed to examine the binding of drugs with α1-acid glycoprotein (AGP). Affinity microcolumns containing immobilized polyclonal anti-AGP antibodies were developed that had a capture efficiency of up to 98.4% for AGP and a binding capacity of 0.72nmol AGP when using a 20mm×2.1mm i.d. microcolumn. These microcolumns were employed in various formats to examine the binding of drugs to normal AGP and AGP that had been adsorbed from serum samples for patients with systemic lupus erythematosus (SLE). Drugs that were screened in zonal elution experiments for their overall binding to these types of AGP included chlorpromazine, disopyramide, imipramine, propranolol, and warfarin. Most of these drugs showed an increase in their binding to the AGP from SLE serum when compared to normal AGP (i.e., an increase of 13-76%); however, disopyramide gave a 21-25% decrease in retention when the same AGP samples were compared. Frontal analysis was used to further evaluate the binding of disopyramide and imipramine to these forms of AGP. Both drugs gave a good fit to a model that involved a combination of saturable and non-saturable interactions with AGP. Changes in the non-saturable interactions accounted for most of variations seen in the binding of disopyramide and imipramine with the AGP samples. The methods used in this study could be adapted for use in personalized medicine and the study of other proteins or drugs using aqueous mixtures or clinical samples.

KW - Alpha-acid glycoprotein

KW - Drug-protein interactions

KW - High-performance affinity chromatography

KW - Immunoextraction

KW - Personalized medicine

KW - Systemic lupus erythematosus

UR - http://www.scopus.com/inward/record.url?scp=85028718429&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85028718429&partnerID=8YFLogxK

U2 - 10.1016/j.chroma.2017.08.073

DO - 10.1016/j.chroma.2017.08.073

M3 - Article

C2 - 28886937

AN - SCOPUS:85028718429

JO - Journal of Chromatography

JF - Journal of Chromatography

SN - 0021-9673

ER -