Thermal investigation of Human Serum Albumin upon Interaction with Ytterbium (III)


Mohammad Mirzaie, Lyla Barzegar, Gholamreza Rezaei Behbehania and Ali Akbar Saboury


In this paper complexation reaction between Yb3+ and Human serum albumin is examined using isothermal titration calorimetry (ITC). The extended solvation model 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.


DOI: j.ccl.2011.12.005

Keywords: Isothermal Titration Calorimetry Human Serum Albumin ,Yb3+ Ion ,Binding Parameters

How to cite this paper:

Mirzaie, M., Barzegar, L., Behbehania, G & Saboury, A. (2012). Thermal investigation of Human Serum Albumin upon Interaction with Ytterbium (III).Current Chemistry Letters, 1(1), 35-40.


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