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

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A Correction to this article was published on 09 February 2019

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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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Change history

  • 09 February 2019

    The authors would like to call the reader?s attention to the following corrections in this article. In the description given for the process of preparing glycated human serum albumin under ?In vitro glycation of HSA?, the concentrations of D-glucose that were employed were 15 mM and 30 mM.

  • 09 February 2019

    The authors would like to call the reader���s attention to the following corrections in this article. In the description given for the process of preparing glycated human serum albumin under ���In vitro glycation of HSA���, the concentrations of D-glucose that were employed were 15 mM and 30 mM.

  • 09 February 2019

    The authors would like to call the reader���s attention to the following corrections in this article. In the description given for the process of preparing glycated human serum albumin under ���In vitro glycation of HSA���, the concentrations of D-glucose that were employed were 15 mM and 30 mM.

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Acknowledgments

This work was funded by the NIH under grant R01 DK069629. R. Matsuda was supported under a fellowship through the Molecular Mechanisms of Disease program at the University of Nebraska.

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Authors and Affiliations

  1. Department of Chemistry, University of Nebraska-Lincoln, Lincoln, NE, 68588-0304, USA

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

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  1. Ryan Matsuda
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  2. Zhao Li
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  3. Xiwei Zheng
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  4. David S. Hage
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Correspondence to David S. Hage.

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Matsuda, R., Li, Z., Zheng, X. et al. Analysis of glipizide binding to normal and glycated human serum albumin by high-performance affinity chromatography. Anal Bioanal Chem 407, 5309–5321 (2015). https://doi.org/10.1007/s00216-015-8688-0

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