Abstract
The interaction of Cu2+ to the first 16 residues of the Alzheimer’s amyloid β peptide, Aβ(1–16) was studied by 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 interactions of Aβ(1–16) with glycine, Gly+Aβ(1–16), and Cu2+ ions, Cu2+ +Aβ(1–16), over the whole range of Cu2+ concentrations. The binding parameters recovered from the solvation model were attributed to the structural change of Aβ(1–16) due to the glycine and Cu2+ interactions. It was found that there is a set of two identical binding sites for Cu2+ ions. p=2 indicates that the binding has positive cooperativity in the two binding sites. Aβ(1–16) structure is destabilized greatly as a result of binding to Cu2+ ions.
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Rezaei Behbehani, G., Mirzaie, M. A high performance method for thermodynamic study on the binding of copper ion and glycine with Alzheimer’s amyloid β peptide. J Therm Anal Calorim 96, 631–635 (2009). https://doi.org/10.1007/s10973-008-9311-9
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DOI: https://doi.org/10.1007/s10973-008-9311-9