Characterization of Amyloid β Fibrils with An Aqueous Two-Phase System: Implications of Fibril Formation

被引:7
|
作者
Shimanouchi, Toshinori [1 ]
Shimauchi, Naoya [1 ]
Nishiyama, Keiichi [1 ]
Vu, Huong Thi [1 ]
Yagi, Hisashi [2 ]
Goto, Yuji [2 ]
Umakoshi, Hiroshi [1 ]
Kuboi, Ryoichi [1 ]
机构
[1] Osaka Univ, Grad Sch Engn Sci, Div Chem Engn, Osaka 5608531, Japan
[2] Osaka Univ, Inst Prot Res, Suita, Osaka 5650871, Japan
基金
日本学术振兴会;
关键词
ASSOCIATION; MECHANISM;
D O I
10.15261/serdj.17.121
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
The pathological process of Alzheimer's disease is closely related to amyloid fibril formation by the causative protein, amyloid beta (A beta). The growth behavior of A beta fibrils is predominated by the seeds-monomeric A beta interaction. In this study, the local hydrophobicity of seeds of A beta fibrils was investigated by the aqueous two-phase partitioning method to evaluate the hydrophobic interaction between the seed-monomeric A beta. The seeds showed a high local hydrophobicity relative to the monomer and fibrils. From the fibril growth experiment and the additive effect of Triton X-100, we could demonstrate the contribution of the hydrophobic seeds-monomer interaction to fibril formation.
引用
收藏
页码:121 / 128
页数:8
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