Thermodynamic Study of Human Serum Albumin upon Interaction with Ytterbium (III)

Thermodynamic Study of Human Serum Albumin upon Interaction with Ytterbium (III)

Complexation reaction between Yb3+ and human serum albumin is examined using isothermal titration calorimetry (ITC). The extension solvation theory was used to reproduce the enthalpies of HAS + Yb3+ interactions over the whole range of Yb3+ concentrations. The binding parameters recovered from this...

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Veröffentlicht in:Journal of chemistry 2012, Vol.2013 (2013), p.1-4
Hauptverfasser: Barzegar, Lyla, Behbehani, Gholamreza Rezaei, Savad Koohi, M. K. Kiani, Mohebbian, M., Abedi, B. Samak, Saboury, Ali Akbar, Divsalar, Adeleh
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container_end_page 4
container_issue 2013
container_start_page 1
container_title Journal of chemistry
container_volume 2013
creator Barzegar, Lyla
Behbehani, Gholamreza Rezaei
Savad Koohi, M. K. Kiani
Mohebbian, M.
Abedi, B. Samak
Saboury, Ali Akbar
Divsalar, Adeleh
description Complexation reaction between Yb3+ and human serum albumin is examined using isothermal titration calorimetry (ITC). The extension solvation theory was used to reproduce the enthalpies of HAS + Yb3+ interactions over the whole range of Yb3+ concentrations. The binding parameters recovered from this model were attributed to the structural change of HSA. The results show that Yb3+ ions bind to HSA with three equivalent affinity sites. It was found that in the high concentrations of the ytterbium ions, the HSA structure was destabilized.
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title Thermodynamic Study of Human Serum Albumin upon Interaction with Ytterbium (III)
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