Cu(Ⅱ) Potentiation of Alzheimer Aβ1-40 Cytotoxicity and Transition on its Secondary Structure

作     者：Xue-Ling DAI~1 Ya-Xuan SUN~2 Zhao-Feng JIANG~2* 1 College of Life Science,Capital Normal University,Beijing 100037,China 2 College of Applied Sciences and Humanities,Beijing Union University,Beijing 100083,China 

作者机构：College of Life Science Capital Normal UniversityBeijing 100037 China College of Applied Sciences and Humanities Beijing Union UniversityBeijing 100083 China 

出 版 物：《Acta Biochimica et Biophysica Sinica》 (生物化学与生物物理学报(英文版))

年 卷 期：2006年第38卷第11期

页      面：765-772页

核心收录：

学科分类：1002[医学-临床医学] 100203[医学-老年医学] 10[医学] 

基　　金：This work was supported by a grant from the Natural Science Foundation of Beijing (No.KZ200311417015) 

主　　题：Alzheimer’s disease Cu(Ⅱ)·Aβ1-40 complex neuron injury Aβ secondary structure 

摘      要：Mounting evidence has shown that dyshomeostasis of the redox-active biometals such as Cuand Fe can lead to oxidative stress,which plays a key role in the neuropathology of Alzheimer s disease（AD）.Here we demonstrate that with the formation of Cu（Ⅱ）·Aβ1-40 complexes,copper markedly potentiatesthe neurotoxicity exhibited by β-amyloid peptide （Aβ）.A greater amount of hydrogen peroxide was releasedwhen Cu（Ⅱ）·Aβ1-40 complexes was added to the xanthine oxidase/xanthine system detected by potassiumiodide *** bound to Aβ1-40 was observed by electron paramagnetic resonance（EPR） *** dichroism （CD） studies indicated that copper chelation could cause a structuraltransition of Aβ.The addition of copper to Aβ introduced an increase on β-sheet as well as α-helix,whichmay be responsible for the aggregation of Aβ.We hypothesized that Aβ aggregation induced by copper maybe responsible for local injury in *** interaction between Cu2+and Aβ also provides a possible mechanismfor the enrichment of metal ions in amyloid plaques in the AD brain.