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Secondary nucleation of Aβ fibrils on liposome membrane

Authors

  • Toshinori Shimanouchi,

    1. Division of Chemical Engineering, Graduate School of Engineering Science, Osaka University, 1-3 Machikaneyama-cho, Toyonaka, Osaka 560-8531, Japan
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  • Nachi Kitaura,

    1. Division of Chemical Engineering, Graduate School of Engineering Science, Osaka University, 1-3 Machikaneyama-cho, Toyonaka, Osaka 560-8531, Japan
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  • Ryo Onishi,

    1. Division of Chemical Engineering, Graduate School of Engineering Science, Osaka University, 1-3 Machikaneyama-cho, Toyonaka, Osaka 560-8531, Japan
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  • Hiroshi Umakoshi,

    Corresponding author
    1. Division of Chemical Engineering, Graduate School of Engineering Science, Osaka University, 1-3 Machikaneyama-cho, Toyonaka, Osaka 560-8531, Japan
    • Division of Chemical Engineering, Graduate School of Engineering Science, Osaka University, 1-3 Machikaneyama-cho, Toyonaka, Osaka 560-8531, Japan===

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  • Ryoichi Kuboi

    1. Division of Chemical Engineering, Graduate School of Engineering Science, Osaka University, 1-3 Machikaneyama-cho, Toyonaka, Osaka 560-8531, Japan
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Abstract

The amyloid fibrils of amyloid β protein (Aβ) from Alzheimer's disease are likely to show the cytotoxicity, depending on their morphology. The relationship between the nucleation kinetics of the Aβ fibrils and their morphology has been investigated. From the perspective of a crystallization technique assuming primary/secondary nucleation steps and an elongation step, the secondary nucleation rate B [# m−3 s−1], was experimentally and coarsely determined by using total internal reflection fluorescence microscopy combined with thioflavin T. In an aqueous solution, linear and rigid fibrils were formed with a relatively smaller B value ((2.83 ± 0.55) × 105 # m−3 s−1), whereas spherulitic amyloid assemblies were formed in the presence of negatively charged liposome including oxidized lipids, with a larger B value ((7.65 ± 0.47) × 105 # m−3 s−1). Those findings should lead to a better understanding of the mechanism for the formation of fibrils and senile plaques in Alzheimer's disease. © 2012 American Institute of Chemical Engineers AIChE J, 2012

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