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Local Atomic Structure and Computer Modeling of the Copper Ion in Amyloid Beta Peptide: XAS Study

Abstract

Local Atomic Structure and Computer Modeling of the Copper Ion in Amyloid Beta Peptide: XAS Study

M.A. Kremennaya, M.A. Soldatov, A.P. Chaynikov, Y.S. Podkovyrina, A.L. Bugaev, K.A. Lomachenko, A.N. Kravtsova

Incoming article date: 30.05.2013

Alzheimer's disease is an incurable illness. It affects about half a million people in Russia, and due to the general trend towards aging of the population the number of Alzheimer's disease cases will steadily increase. Insoluble deposits of amyloid beta in the brain tissue (amyloid plaques) are the major morphological characteristic of Alzheimer's disease. It has been found that the increased concentration of copper in amyloid plaques results in copper ions bound to the protein. It is the presence of copper in the binding site triggers of the formation of amyloid plaques. Therefore, the study of the binding site in amyloid beta is of great scientific interest. The local atomic structure of the Cu(I) copper ion binding site in the amyloid beta peptide has been studied by means of XANES spectroscopy. Several model structures obtained by molecular mechanics and density functional theory (ADF code) have been tested. Theoretical analysis of X-ray absorption spectra based on the finite difference method implemented in FDMNES code was performed. An appropriate model structure of the Cu(I) copper ion binding site in amyloid beta peptide has been found.

Keywords: amyloid beta, binding site, Alzheimer's disease, the method of finite differences, Cu(I)