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

Toshinori Shimanouchi, Naoya Shimauchi, Keiichi Nishiyama, Huong Thi Vu, Hiroshi Umakoshi, Ryoichi Kuboi, Hisashi Yagi, Yuji Goto

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

The pathological process of Alzheimer's disease is closely related to amyloid fibril formation by the causative protein, amyloid β (Aβ). The growth behavior of Aβ fibrils is predominated by the seeds-monomeric Aβ interaction. In this study, the local hydrophobicity of seeds of Aβ fibrils was investigated by the aqueous two-phase partitioning method to evaluate the hydrophobic interaction between the seed-monomeric Aβ. 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.

Original languageEnglish
Pages (from-to)121-128
Number of pages8
JournalSolvent Extraction Research and Development
Volume17
DOIs
Publication statusPublished - Jan 1 2010
Externally publishedYes

ASJC Scopus subject areas

  • Chemistry(all)
  • Chemical Engineering(all)

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