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

  • Articles/Chembiology
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Chinese Science Bulletin

Abstract

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.

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Authors and Affiliations

  1. Chemistry Department, Imam Khomeini International University, Qazvin, Iran

    Rezaei G. Behbehani

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  1. Rezaei G. Behbehani
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Correspondence to Rezaei G. Behbehani.

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

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Behbehani, R.G. A novel method for thermodynamic study on binding of copper ion with Alzheimer’s amyliod β peptide. Chin. Sci. Bull. 54, 1037–1042 (2009). https://doi.org/10.1007/s11434-009-0065-y

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  • DOI: https://doi.org/10.1007/s11434-009-0065-y

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