TY - JOUR
T1 - Characterization of Amyloid β Fibrils with An Aqueous Two-Phase System
T2 - Implications of Fibril Formation
AU - Shimanouchi, Toshinori
AU - Shimauchi, Naoya
AU - Nishiyama, Keiichi
AU - Vu, Huong Thi
AU - Umakoshi, Hiroshi
AU - Kuboi, Ryoichi
AU - Yagi, Hisashi
AU - Goto, Yuji
PY - 2010
Y1 - 2010
N2 - 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.
AB - 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.
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U2 - 10.15261/serdj.17.121
DO - 10.15261/serdj.17.121
M3 - Article
AN - SCOPUS:78649673848
SN - 1341-7215
VL - 17
SP - 121
EP - 128
JO - Solvent Extraction Research and Development
JF - Solvent Extraction Research and Development
ER -