A12 超音波による蛋白質溶液の過飽和解消とアミロイド線維形成(口頭発表)

DOI

書誌事項

タイトル別名
  • A12 Ultrasonication-dependent breakdown of protein supersaturation and formation of amyloid fibrils

抄録

Amyloid fibrils are associated with various serious diseases such as Alzheimer's disease and type II diabetes. We reported that ultrasonication is useful for inducing amyloid nucleation and thus the formation of fibrils. In this paper, we studied the effects of various alcohols in inducing amyloid fibrils. The results indicate that, although fibrillation is determined by solubility, supersaturation prevents conformational transition and that ultrasonication is effective in breaking supersaturation. We propose an alcohol-dependent protein misfolding funnel useful for examining the amyloidogenicity. Second, to perform a high throughput analysis of the formation of amyloid fibrils, we developed a HANABI system, in which a fluorescence microplate reader was combined with a water-bath-type ultrasonicator. Third, with HANABI, we succeeded in detecting the ultrasonication-accelerated formation of protein crystals as well as amyloid fibrils. Taken together, ultrasonication will become a unique technology for characterizing various types of supersaturation of protein solution, leading to understanding the role of supersaturation in life.

収録刊行物

キーワード

詳細情報 詳細情報について

  • CRID
    1390282681028746752
  • NII論文ID
    110009732815
  • DOI
    10.20577/pamjss.22.0_107
  • ISSN
    24241512
  • 本文言語コード
    ja
  • データソース種別
    • JaLC
    • CiNii Articles
  • 抄録ライセンスフラグ
    使用不可

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