A High Performance Theory for Thermodynamic Study on the Binding of Human Serum Albumin with Erbium Chloride

作者：Behbehani G Rezaei^*; Divsalar A; Saboury A A; Faridbod F; Ganjali M R

来源：Chinese Journal of Chemistry, 2009, 27(2): 289-294.

DOI：10.1002/cjoc.200990046

• human serum albumin
• isothermal titration calorimetry
• erbium(III) chloride
• binding site

A thermodynamic study of the interaction between erbium(III) chloride (Er(3 )) and human serum albumin (HSA) was Studied at pH=7.0, 27 and 37 degrees C in phosphate buffer by isothermal titration calorimetry (ITC). The present study reports the thermodynamic parameters that govern HSA-Er(3 ) interactions. The extended solvation theory was used to reproduce the enthalpies of HSA-Er(3 ) interactions over the whole range of Er(3 ) concentrations. The binding parameters recovered from the new model were attributed to the structural change of HSA and its biological activity. The results obtained indicate that there is a set of two identical binding sites for Er(3 ) ions with negative cooperativity. The enhancement of complex formation by Er(3 ) and concomitant increase in AS Suggest that the metal ion plays a role in increasing the number of hydrophobic contacts. The binding parameters discovered from the extended solvation model indicate that the stability of HSA molecule is increased as a result of its interaction with Er(3 ) ions.

• 出版日期2009-2