Amyloid-β peptide aggregation and the influence of carbon nanoparticles

doi:10.1088/1674-1056/25/1/018704

Abstract 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.

Keywords: Amyloid-β oligomerization carbon nanoparticles molecular dynamics

Received: 12 May 2015
Revised: 16 August 2015
Accepted manuscript online:

PACS:	87.14.em	(Fibrils (amyloids, collagen, etc.))
	87.15.nr	(Aggregation)
	87.15.bk	(Structure of aggregates)
	87.15.ap	(Molecular dynamics simulation)

Fund: Project supported by the National Natural Science Foundation of China (Grant Nos. 11274075 and 91227102).

Corresponding Authors: Guang-Hong Wei
E-mail: ghwei@fudan.edu.cn

Cite this article:

Wen-Hui Xi(郗文辉) and Guang-Hong Wei(韦广红) Amyloid-β peptide aggregation and the influence of carbon nanoparticles 2016 Chin. Phys. B 25 018704

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Amyloid-β peptide aggregation and the influence of carbon nanoparticles

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