Influence of Au nanoparticles on the aggregation of amyloid-β-(25-35) peptides

被引：49

作者：

Ma, Qianqian

Wei, Guanghong

Yang, Xinju ^{[1
]}

机构：

[1] Fudan Univ, State Key Lab Surface Phys, Shanghai 200433, Peoples R China

来源：

NANOSCALE | 2013年 / 5卷 / 21期

基金：

中国国家自然科学基金; 上海市自然科学基金;

关键词：

CARBON NANOTUBE; GOLD NANOPARTICLES; ALZHEIMERS-DISEASE; WORK FUNCTION; BETA-PEPTIDE; ADSORPTION; SURFACE; A-BETA(1-42); INHIBITION; OLIGOMERS;

D O I：

10.1039/c3nr02973e

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

The influence of Au nanoparticles (Au NPs) on the aggregation of amyloid-beta-(25-35) peptides (A beta(25-35)) is investigated by atomic force microscopy and Thioflavin T fluorescence measurements. It is found that, without Au NPs, the A beta(25-35) peptides aggregate gradually from monomers and oligomers to long fibrils with the incubation time. In contrast, short protofibrils are formed quickly after Au NPs are added to the A beta(25-35) solution, which can be further aggregated to form short fibril bundles or even bundle conjunctions. To reveal the origin of Au NPs on the aggregation of A beta(25-35), electrostatic force microscopy and scanning Kelvin microscopy are employed to investigate the electrical properties of the A beta(25-35) fibrils with and without Au NPs. Due to the significant difference of the electrical properties between the A beta(25-35) fibrils and Au NPs, the locations of Au NPs inside the A beta(25-35) fibril bundles can be revealed and hence a possible influence mechanism of Au NPs on the aggregation of A beta(25-35) is suggested.

引用

页码：10397 / 10403

页数：7

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