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

A thermodynamic study of the interaction between erbium(Ⅲ) chloride (Er3+) and human serum albumin (HAS) was studied at pH=7.0, 27 and 37℃ in phosphate buffer by isothermal titration calorimetry (ITC). The present study reports the thermodynamic parameters that govern HAS-Er3+ interactions. The extended solvation theory was used to reproduce the enthalpies of HAS-Er3+ interactions over the whole range of Er3+ concentrations. The bind-ing parameters recovered from the new model were attributed to the structural change of HAS and its biological ac-tivity. The results obtained indicate that there is a set of two identical binding sites for Er3+ ions with negative co-operativity. The enhancement of complex formation by Er3+ and concomitant increase in △S suggest that the metal ion plays a role in increasing the number of hydrophobic contacts. The binding parameters discovered from the ex-tended solvation model indicate that the stability of HAS molecule is increased as a result of its interaction with Er3+ ions.

作 者： BEHBEHANI G Rezaei DIVSALAR A SABOURY A. A FARIDBOD, F GANJALI M R   作者單位： BEHBEHANI G Rezaei(Chemistry Department,Imam Khomeini International University,Qazvin,Iran)

DIVSALAR A(Institute of Biochemistry and Biophysics,University of Tehran,Tehran,Iran;Department of Biological Sciences,Tarbiat Moallem University,Tehran,Iran)

SABOURY A. A(Institute of Biochemistry and Biophysics,University of Tehran,Tehran,Iran)

FARIDBOD, F,GANJALI M R(Departments of Chemistry,University of Tehran,Tehran,Iran) 

刊 名： 中國化學(xué)（英文版）  SCI 英文刊名： CHINESE JOURNAL OF CHEMISTRY  年，卷(期)： 2009 27(2)  分類號： O6  關(guān)鍵詞： human serum albumin   isothermal titration calorimetry   erbium(Ⅲ) chloride   binding site  

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