Characterization of amyloid β fibrils with an aqueous two-phase system: Implications of fibril formation

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

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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
Publication statusPublished - 2010
Externally publishedYes

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ASJC Scopus subject areas

  • Chemistry(all)
  • Chemical Engineering(all)

Cite this

Shimanouchi, T., Shimauchi, N., Nishiyama, K., Vu, H. T., Yagi, H., Goto, Y., Umakoshi, H., & Kuboi, R. (2010). Characterization of amyloid β fibrils with an aqueous two-phase system: Implications of fibril formation. Solvent Extraction Research and Development, 17, 121-128.