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

来源：

SOLVENT EXTRACTION RESEARCH AND DEVELOPMENT-JAPAN | 2010年 / 17卷

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

页码：121 / 128

页数：8

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