%0 Journal Article
%T A novel method for thermodynamic study on binding of copper ion with Alzheimer’s amyliod β peptide<br>
%A Rezaei G Behbehani
%A <br>
%J 科学通报(英文版)
%D 2009
%I 
%X 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°C 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. Supported by the University of Imam Khomeini (Qazvin) and University of Tehran and Iranian National Science Foundation (INSF)
%K Alzheimer’
%K s amyliod β
%K peptide
%K isothermal titration calorimetry
%K solvation parameters<br>
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=01BA20E8BA813E1908F3698710BBFEFEE816345F465FEBA5&cid=96E6E851B5104576C2DD9FC1FBCB69EF&jid=DD6615BC9D2CFCE0B6F945E8D5314523&aid=F284A69AB9C523E51394A99DABA1D56F&yid=DE12191FBD62783C&vid=318E4CC20AED4940&iid=B31275AF3241DB2D&sid=1F51A4E3D1D75885&eid=9E5DBB98644FDC52&journal_id=1001-6538&journal_name=科学通报(英文版)&referenced_num=0&reference_num=35