| Molecular dynamics studies of the inhibitory mechanism of copper（Ⅱ） on aggregation of amyloid β-peptide |
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| 作者姓名： | Yong Jiao Pin Yang |
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| 作者单位： | Institute of Molecular Science, Key Laboratory of Chemical Biology and Molecular Engineering of Ministry of Education, Shanxi University, Taiyuan 030006, China |
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| 基金项目： | Acknowledgments This work was supported by the National Natural Science Foundation of China （Nos. 30470408 and 20637010）. |
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| 摘 要： | The inhibitory mechanism of copper（Ⅱ） on the aggegation of amyloid β-peptide （Aβ） was investigated by molecular dynamics simulations. The binding mode ofcopper（Ⅱ） with Aβ is characterized by the imidazole nitrogen atom, Nπ, of the histidine residue H 13, acting as the anchoring site, and the backbone＇s deprotoned amide nitogen atoms as the main binding sites. Drove by the coordination bonds and their induced hydrogen bond net, the conformations of Aβ converted from β-sheet non-β-sheet conformations, which destabilized the aggregation of Aβ into fibrils.
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| 关 键 词： | 二价铜 淀粉样β-肽 聚合 抑制作用 机理 分子动力学 |
| 收稿时间： | 2006-08-31 |
Molecular dynamics studies of the inhibitory mechanism of copper(II) on aggregation of amyloid β-peptide |
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| Yong Jiao Pin Yang.Molecular dynamics studies of the inhibitory mechanism of copper(II) on aggregation of amyloid β-peptide[J].Chinese Chemical Letters,2007,18(3):357-360. |
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| Authors: | Yong Jiao Pin Yang |
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| Institution: | Institute of Molecular Science, Key Laboratory of Chemical Biology and Molecular Engineering of Ministry of Education, Shanxi University, Taiyuan 030006, China |
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| Abstract: | The inhibitory mechanism of copper(II) on the aggregation of amyloid β-peptide (Aβ) was investigated by molecular dynamics simulations. The binding mode of copper(II) with Aβ is characterized by the imidazole nitrogen atom, Nπ, of the histidine residue H13, acting as the anchoring site, and the backbone's deprotoned amide nitrogen atoms as the main binding sites. Drove by the coordination bonds and their induced hydrogen bond net, the conformations of Aβ converted from β-sheet non-β-sheet conformations, which destabilized the aggregation of Aβ into fibrils. |
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