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The Structural Study of Copper-binding Peptides: Implication in the Aggregation of Amyloid-β Peptides

By Ren-Jie Lin, Tzyy-Rong Jinn, Soonmin Jang, Fur-Der Mai and Feng-Yin Li

Abstract

There is evidence that copper is bound to amyloid-β peptide (Aβ) in senile plaque of Alzheimer's disease. Copper also plays a role in the neurotoxicity of the Aβ aggregates associated with free radical damage. In this study, we used L-histidyl-L-histidine peptide (di-histidine) to represent Aβ along with ab initio calculation to characterize the probable coordination between Cu(II) and Aβs to explore the Aβ aggregate structures. Sixteen models of copper-di-histidine complexes were proposed to investigate the copper-induced aggregation of Aβs through copper ionic coordination. All structures of the proposed models were optimized at the M05-2X/LanL2DZ level, and an Aβ aggregation formation mechanism was proposed

Topics: Amyloid-β peptide, Metal chelation, Amyloid aggregation, Density functional theory
Year: 2014
DOI identifier: 10.1002/jccs.201300086
OAI identifier: oai:ir.lib.nchu.edu.tw:11455/84984
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