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Phys Chem Chem Phys. 2019 Jan 9. doi: 10.1039/c8cp07211f. [Epub ahead of print]

Aggregation of amyloid peptides into fibrils driven by nanoparticles and their curvature effect.

Author information

1
Laboratory of Theoretical and Computational Nanoscience, CAS Key Laboratory of Nanosystem and Hierarchy Fabrication, CAS Center for Excellence in Nanoscience, National Center for Nanoscience and Technology, Chinese Academy of Sciences, Beijing 100190, P. R. China. shixh@nanoctr.cn.
2
State Key Laboratory of Polymer Physics and Chemistry, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun 130022, P. R. China.
3
Laboratory of Theoretical and Computational Nanoscience, CAS Key Laboratory of Nanosystem and Hierarchy Fabrication, CAS Center for Excellence in Nanoscience, National Center for Nanoscience and Technology, Chinese Academy of Sciences, Beijing 100190, P. R. China. shixh@nanoctr.cn and University of Chinese Academy of Sciences, Beijing 100049, P. R. China.

Abstract

Fibrillation of amyloid peptides induces human diseases such as Alzheimer's disease, which has become a huge challenge. Some nanoparticles (NPs) could enhance peptide fibrillation by decreasing the lag time, yet how the size and shape of NPs affect amyloid fibrillation as well as the underlying mechanism remains unclear. Here, we investigated amyloid fibrillation on the surface of spherical NPs and cylindrical nanorods (NRs) of different sizes using coarse-grained Monte Carlo simulations. We focused on the curvature effect of NPs/NRs on the adsorption and fibrillation of peptide chains due to the size/shape difference. As the size of the NPs/NRs increases, the number of assembled peptide chains shows a non-monotonic tendency, and there is an optimal size for the highest adsorption. In most cases, the NRs could adsorb more peptides than the NPs of the same diameter due to the lower curvature. The mechanism beneath these observations was elucidated from a thermodynamic point of view. Our findings could provide a physical basis for the adsorption and fibrillation of amyloid peptides on NPs, and guide the design of future curvature-dependent NP-based amyloid treatment.

PMID:
30624452
DOI:
10.1039/c8cp07211f

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