| Amyloid-β peptide aggregation and the influence of carbon nanoparticles |
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| 作者姓名： | 郗文辉 韦广红 |
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| 作者单位： | Key Laboratory for Computational Physical Sciences (Ministry of Education), State Key Laboratory of Surface Physics, Department of Physics, Fudan University, Shanghai 200433, China |
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| 基金项目： | Project supported by the National Natural Science Foundation of China (Grant Nos. 11274075 and 91227102). |
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| 摘 要： | Soluble peptides or proteins can self-aggregate into insoluble, ordered amyloid fibrils under appropriate conditions.These amyloid aggregates are the hallmarks of several human diseases ranging from neurodegenerative disorders to systemic amyloidoses. In this review, we first introduce the common structural features of amyloid fibrils and the amyloid fibrillation kinetics determined from experimental studies. Then, we discuss the structural models of Alzheimer's amyloid-β(Aβ) fibrils derived from solid-state nuclear magnetic resonance spectroscopy. On the computational side, molecular dynamics simulations can provide atomic details of structures and the underlying oligomerization mechanisms. We finally summarize recent progress in atomistic simulation studies on the oligomerization of Aβ(including full-length Aβ and its fragments) and the influence of carbon nanoparticles.
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| 收稿时间： | 2015-05-12 |
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