A novel method for thermodynamic study on binding of copper ion with Alzheimer’s amyliod β peptide  

作　　者：BEHBEHANI G. Rezaei 

机构地区：[1]Chemistry Department, Imam Khomeini International University

出　　处：《Chinese Science Bulletin》2009年第6期1037-1042,共6页

基　　金：Supported by the University of Imam Khomeini (Qazvin)and University of Tehran and Iranian National Science Foundation (INSF)

摘　　要：The interaction of Cu2+ with the first 16 residues of the Alzheimer's amyliod β peptide, Aβ (1-16), was studied by employing isothermal titration calorimetry at pH 7.2 and 37℃ in aqueous solution. The Gholamreza Rezaei Behbehani (GRB) solvation model was used to reproduce the enthalpies of Cu2++ Aβ(1-16) interaction over the whole Cu2+ concentrations. The binding parameters recovered from the solvation model were attributed to the structural change of Aβ (1-16) due to the metal ion interaction. It was found that there is a set of two identical and non interacting binding sites for Cu2+ ions. The molar enthalpy of binding is ΔH=27.895 kJ/mol. The association binding constants are 1.895 μM-1 and 1.891 μM-1 for the first and second binding sites respectively.The interaction of Cu^2＋ with the first 16 residues of the Alzheimer＇s amyliod ,8 peptide, Aβ（1-16）, was studied by employing isothermal titration calorimetry at pH 7.2 and 37℃ in aqueous solution. The Gholamreza Rezaei Behbehani （GRB） solvation model was used to reproduce the enthalpies of Cu^2＋ ＋ Aβ（1-16） interaction over the whole Cu^2＋ concentrations. The binding parameters recovered from the solvation model were attributed to the structural change of Aβ（1-16） due to the metal ion interaction. It was found that there is a set of two identical and non interacting binding sites for Cu^2＋ ions. The molar enthalpy of binding is △H=27.895 kJ/mol. The association binding constants are 1.895 μM^-1 and 1.891 μM^-1 for the first and second binding sites respectively.

关 键 词：阿尔茨海默氏症 铜离子 热力学 等温滴定量热法 相互作用 肽 结合位点 摩尔焓 

分 类 号：R749.16[医药卫生—神经病学与精神病学]