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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| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Wiley
2013-01-01
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| Series: | Journal of Chemistry |
| Online Access: | http://dx.doi.org/10.1155/2013/696394 |
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| Summary: | 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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| ISSN: | 2090-9063 2090-9071 |