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
收藏
页码：10397 / 10403
页数：7
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