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The Structural Study of Copper‐binding Peptides: Implication in the Aggregation of Amyloid‐β Peptides
Author(s) -
Lin RenJie,
Jinn TzyyRong,
Jang Soonmin,
Mai FurDer,
Li FengYin
Publication year - 2013
Publication title -
journal of the chinese chemical society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.329
H-Index - 45
eISSN - 2192-6549
pISSN - 0009-4536
DOI - 10.1002/jccs.201300086
Subject(s) - chemistry , copper , histidine , peptide , senile plaques , neurotoxicity , ab initio , amyloid (mycology) , amyloid β , biophysics , crystallography , alzheimer's disease , biochemistry , inorganic chemistry , organic chemistry , amino acid , toxicity , disease , pathology , medicine , biology
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.