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Issue 45, 2017, Issue in Progress
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Interaction of human serum albumin with uremic toxins: a thermodynamic study

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Abstract

We present a comprehensive study of the interaction of human serum albumin (HSA) with two uremic toxins, namely phenylacetic acid (PhAA) and indoxyl sulfate (IDS) in aqueous solution. The interaction of HSA with PhAA is studied for a series of salt concentrations (20–150 mM) and temperature (25, 30 and 37 °C). The effect of in vitro urea modification of HSA upon its binding affinity towards the uremic toxins, is studied under the highest and lowest salt concentrations and the different temperatures. Isothermal titration calorimetry (ITC) is used to study the interaction by analyzing binding affinities and related thermodynamic data. It is found that two PhAA molecules bind to HSA in a sequential binding process with a binding constant kb in the order of ≈104 and ≈103 for the first and second binding respectively. In contrast, IDS binds much stronger to HSA with a total of ≈3 molecules to a high and low affinity binding site in the order of ≈105 and ≈103. Binding of uremic toxins to HSA in all cases show a decreasing binding affinity trend with increasing temperature and higher ionic strength. Thus binding of a second uremic toxin is strongly weakened at 37 °C and 150 mM. Urea induced HSA modification have only minor effect on the binding interaction of the uremic toxins.

Graphical abstract: Interaction of human serum albumin with uremic toxins: a thermodynamic study

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Publication details

The article was received on 08 Mar 2017, accepted on 19 May 2017 and first published on 25 May 2017


Article type: Paper
DOI: 10.1039/C7RA02838E
Citation: RSC Adv., 2017,7, 27913-27922
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    Interaction of human serum albumin with uremic toxins: a thermodynamic study

    S. Yu, M. Schuchardt, M. Tölle, M. van der Giet, W. Zidek, J. Dzubiella and M. Ballauff, RSC Adv., 2017, 7, 27913
    DOI: 10.1039/C7RA02838E

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