Analysis of glipizide binding to normal and glycated human serum albumin by high-performance affinity chromatography

Ryan Matsuda, Zhao Li, Xiwei Zheng, David S. Hage

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

Abstract In diabetes, the elevated levels of glucose in the bloodstream can result in the nonenzymatic glycation of proteins such as human serum albumin (HSA). This type of modification has been shown to affect the interactions of some drugs with HSA, including several sulfonylurea drugs that are used to treat type II diabetes. This study used high-performance affinity chromatography (HPAC) to examine the interactions of glipizide (i.e., a second-generation sulfonylurea drug) with normal HSA or HSA that contained various levels of in vitro glycation. Frontal analysis indicated that glipizide was interacting with both normal and glycated HSA through two general groups of sites: a set of relatively strong interactions and a set of weaker interactions with average association equilibrium constants at pH 7.4 and 37°C in the range of 2.4-6.0 × 105 and 1.7-3.7 × 104 M-1, respectively. Zonal elution competition studies revealed that glipizide was interacting at both Sudlow sites I and II, which were estimated to have affinities of 3.2-3.9 × 105 and 1.1-1.4 × 104 M-1. Allosteric effects were also noted to occur for this drug between the tamoxifen site and the binding of R-warfarin at Sudlow site I. Up to an 18 % decrease in the affinity for glipizide was observed at Sudlow site I ongoing from normal HSA to glycated HSA, while up to a 27 % increase was noted at Sudlow site II. This information should be useful in indicating how HPAC can be used to investigate other drugs that have complex interactions with proteins. These results should also be valuable in providing a better understanding of how glycation may affect drug-protein interactions and the serum transport of drugs such as glipizide during diabetes.

Original languageEnglish (US)
Article number8688
Pages (from-to)5309-5321
Number of pages13
JournalAnalytical and Bioanalytical Chemistry
Volume407
Issue number18
DOIs
StatePublished - Jul 28 2015

Fingerprint

Glipizide
Affinity chromatography
Affinity Chromatography
Serum Albumin
Pharmaceutical Preparations
Medical problems
Drug Interactions
Proteins
Equilibrium constants
Warfarin
Tamoxifen
Type 2 Diabetes Mellitus
Blood Proteins
Binding Sites
Association reactions
Glucose

Keywords

  • Drug-protein binding
  • Glipizide
  • Glycation
  • High-performance affinity chromatography
  • Human serum albumin

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry

Cite this

Analysis of glipizide binding to normal and glycated human serum albumin by high-performance affinity chromatography. / Matsuda, Ryan; Li, Zhao; Zheng, Xiwei; Hage, David S.

In: Analytical and Bioanalytical Chemistry, Vol. 407, No. 18, 8688, 28.07.2015, p. 5309-5321.

Research output: Contribution to journalArticle

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N2 - Abstract In diabetes, the elevated levels of glucose in the bloodstream can result in the nonenzymatic glycation of proteins such as human serum albumin (HSA). This type of modification has been shown to affect the interactions of some drugs with HSA, including several sulfonylurea drugs that are used to treat type II diabetes. This study used high-performance affinity chromatography (HPAC) to examine the interactions of glipizide (i.e., a second-generation sulfonylurea drug) with normal HSA or HSA that contained various levels of in vitro glycation. Frontal analysis indicated that glipizide was interacting with both normal and glycated HSA through two general groups of sites: a set of relatively strong interactions and a set of weaker interactions with average association equilibrium constants at pH 7.4 and 37°C in the range of 2.4-6.0 × 105 and 1.7-3.7 × 104 M-1, respectively. Zonal elution competition studies revealed that glipizide was interacting at both Sudlow sites I and II, which were estimated to have affinities of 3.2-3.9 × 105 and 1.1-1.4 × 104 M-1. Allosteric effects were also noted to occur for this drug between the tamoxifen site and the binding of R-warfarin at Sudlow site I. Up to an 18 % decrease in the affinity for glipizide was observed at Sudlow site I ongoing from normal HSA to glycated HSA, while up to a 27 % increase was noted at Sudlow site II. This information should be useful in indicating how HPAC can be used to investigate other drugs that have complex interactions with proteins. These results should also be valuable in providing a better understanding of how glycation may affect drug-protein interactions and the serum transport of drugs such as glipizide during diabetes.

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