Nanoscale insights into full-length prion protein aggregation on model lipid membranes

被引：6
|
作者：
Pan, Yangang [1 ,2 ]
Wang, Bin [1 ,2 ]
Zhang, Tong [1 ,2 ]
Zhang, Yanan [1 ,2 ]
Wang, Hongda [3 ]
Xu, Bingqian [1 ,2 ]
机构：
[1] Univ Georgia, Single Mol Study Lab, Fac Engn, Athens, GA 30602 USA
[2] Univ Georgia, Nanoscale Sci & Engn Ctr, Athens, GA 30602 USA
[3] Chinese Acad Sci, Changchun Inst Appl Chem, State Key Lab Electroanal Chem, Changchun 130022, Jilin, Peoples R China
来源：
CHEMICAL COMMUNICATIONS | 2016年 / 52卷 / 55期
基金：
美国国家科学基金会;
关键词：
BETA-OLIGOMERS; FORCE; PHOSPHATIDYLSERINE; MOLECULES; BILAYERS; CELLS; NEUROTOXICITY; MICROSCOPY; TOXICITY; DISEASE;
D O I：
10.1039/c6cc03029g
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
The aggregates of the full-length human recombinant prion protein (PrP) (23-231) onmodelmembranes were investigated by combining the atomic force microscopy (AFM) measurements and theoretical calculations at pH 5.0, showing the great effect of PrP concentration on its supramolecular assemblies on the lipid bilayer.
引用
收藏
页码：8533 / 8536
页数：4
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