Chromatographic studies of changes in binding of sulfonylurea drugs to human serum albumin due to glycation and fatty acids

Sara B.G. Basiaga, David S Hage

Research output: Contribution to journalArticle

23 Citations (Scopus)

Abstract

This report examines the use of high-performance affinity chromatography as a screening tool for studying the change in binding by sulfonylurea drugs to the protein human serum albumin (HSA) during diabetes. The effects of both the non-enzymatic glycation of HSA and the presence of fatty acids on these interactions were considered using a zonal elution format. It was found that there was a significant increase (i.e., 2.7- to 3.6-fold) in the relative retention of several sulfonylurea drugs (i.e., acetohexamide, tolbutamide, glybenclamide and gliclazide) on columns containing normal versus glycated HSA. The addition of various long chain fatty acids to the mobile phase gave the same trend in retention for the tested drugs on both the HSA and glycated HSA columns, generally leading to lower binding. Most of the fatty acids examined produced similar or moderately different relative shifts in retention; however, palmitic acid was found to produce a much larger change in retention on columns containing glycated HSA versus normal HSA under the conditions used in this study.

Original languageEnglish (US)
Pages (from-to)3193-3197
Number of pages5
JournalJournal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences
Volume878
Issue number30
DOIs
StatePublished - Nov 15 2010

Fingerprint

Serum Albumin
Fatty Acids
Pharmaceutical Preparations
Acetohexamide
Gliclazide
Affinity chromatography
Tolbutamide
Palmitic Acid
Glyburide
Medical problems
Affinity Chromatography
Screening
Proteins

Keywords

  • Drug-protein binding
  • Fatty acids
  • Glycation
  • High-performance affinity chromatography
  • Human serum albumin
  • Sulfonylurea drugs

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry
  • Clinical Biochemistry
  • Cell Biology

Cite this

@article{a788069118d84f7eb3861e9498a0e29b,
title = "Chromatographic studies of changes in binding of sulfonylurea drugs to human serum albumin due to glycation and fatty acids",
abstract = "This report examines the use of high-performance affinity chromatography as a screening tool for studying the change in binding by sulfonylurea drugs to the protein human serum albumin (HSA) during diabetes. The effects of both the non-enzymatic glycation of HSA and the presence of fatty acids on these interactions were considered using a zonal elution format. It was found that there was a significant increase (i.e., 2.7- to 3.6-fold) in the relative retention of several sulfonylurea drugs (i.e., acetohexamide, tolbutamide, glybenclamide and gliclazide) on columns containing normal versus glycated HSA. The addition of various long chain fatty acids to the mobile phase gave the same trend in retention for the tested drugs on both the HSA and glycated HSA columns, generally leading to lower binding. Most of the fatty acids examined produced similar or moderately different relative shifts in retention; however, palmitic acid was found to produce a much larger change in retention on columns containing glycated HSA versus normal HSA under the conditions used in this study.",
keywords = "Drug-protein binding, Fatty acids, Glycation, High-performance affinity chromatography, Human serum albumin, Sulfonylurea drugs",
author = "Basiaga, {Sara B.G.} and Hage, {David S}",
year = "2010",
month = "11",
day = "15",
doi = "10.1016/j.jchromb.2010.09.033",
language = "English (US)",
volume = "878",
pages = "3193--3197",
journal = "Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences",
issn = "1570-0232",
publisher = "Elsevier",
number = "30",

}

TY - JOUR

T1 - Chromatographic studies of changes in binding of sulfonylurea drugs to human serum albumin due to glycation and fatty acids

AU - Basiaga, Sara B.G.

AU - Hage, David S

PY - 2010/11/15

Y1 - 2010/11/15

N2 - This report examines the use of high-performance affinity chromatography as a screening tool for studying the change in binding by sulfonylurea drugs to the protein human serum albumin (HSA) during diabetes. The effects of both the non-enzymatic glycation of HSA and the presence of fatty acids on these interactions were considered using a zonal elution format. It was found that there was a significant increase (i.e., 2.7- to 3.6-fold) in the relative retention of several sulfonylurea drugs (i.e., acetohexamide, tolbutamide, glybenclamide and gliclazide) on columns containing normal versus glycated HSA. The addition of various long chain fatty acids to the mobile phase gave the same trend in retention for the tested drugs on both the HSA and glycated HSA columns, generally leading to lower binding. Most of the fatty acids examined produced similar or moderately different relative shifts in retention; however, palmitic acid was found to produce a much larger change in retention on columns containing glycated HSA versus normal HSA under the conditions used in this study.

AB - This report examines the use of high-performance affinity chromatography as a screening tool for studying the change in binding by sulfonylurea drugs to the protein human serum albumin (HSA) during diabetes. The effects of both the non-enzymatic glycation of HSA and the presence of fatty acids on these interactions were considered using a zonal elution format. It was found that there was a significant increase (i.e., 2.7- to 3.6-fold) in the relative retention of several sulfonylurea drugs (i.e., acetohexamide, tolbutamide, glybenclamide and gliclazide) on columns containing normal versus glycated HSA. The addition of various long chain fatty acids to the mobile phase gave the same trend in retention for the tested drugs on both the HSA and glycated HSA columns, generally leading to lower binding. Most of the fatty acids examined produced similar or moderately different relative shifts in retention; however, palmitic acid was found to produce a much larger change in retention on columns containing glycated HSA versus normal HSA under the conditions used in this study.

KW - Drug-protein binding

KW - Fatty acids

KW - Glycation

KW - High-performance affinity chromatography

KW - Human serum albumin

KW - Sulfonylurea drugs

UR - http://www.scopus.com/inward/record.url?scp=78049474504&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=78049474504&partnerID=8YFLogxK

U2 - 10.1016/j.jchromb.2010.09.033

DO - 10.1016/j.jchromb.2010.09.033

M3 - Article

VL - 878

SP - 3193

EP - 3197

JO - Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences

JF - Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences

SN - 1570-0232

IS - 30

ER -