Amyloid-β peptide aggregation and the influence of carbon nanoparticles*
Amyloid-β peptide aggregation and the influence of carbon nanoparticles*
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DOI：
10.1088/1674-1056/25/1/018704
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发表时间：
2016
影响因子：
1.7
通讯作者：
Wenhui Xi;Guanghong Wei
中科院分区：
文献类型：
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作者：
Wenhui Xi;Guanghong Wei
在适当的条件下，可溶性多肽或蛋白质可以自聚集成不溶的有序淀粉样蛋白原纤维。这些淀粉样蛋白聚集体是几种人类疾病的标志，从神经退行性疾病到全身性淀粉样病变。在这篇综述中，我们首先介绍了淀粉样蛋白原纤维的共同结构特征和实验研究确定的淀粉样蛋白颤动动力学。然后，我们讨论了来自固态核磁共振波谱的阿尔茨海默病淀粉样蛋白-β (Aβ)原纤维的结构模型。在计算方面，分子动力学模拟可以提供结构的原子细节和潜在的寡聚化机制。最后总结了Aβ（包括全长Aβ及其片段）寡聚化原子模拟研究的最新进展以及碳纳米颗粒的影响。
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.