A7 超音波による蛋白質のアミロイド線維形成反応の促進機構(口頭発表)

• 宗 正智

  阪大蛋白研

• 後藤 祐児

  阪大蛋白研

• 荻 博次

  阪大院基礎工

書誌事項

タイトル別名

• A7 The mechanisms of ultrasonication-induced acceleration of amyloid fibril formation

抄録

Amyloid fibrils are highly ordered assemblies of misfolded proteins associated with over 30 degenerative diseases including Alzheimer's diseases or type 2 diabetes. Fibrils, similar to crystals, form through nucleation and growth in a supersaturated solution. Fibril formation takes a long time because of the high free-energy barrier of nucleation. Ultrasonic irradiation is one of the most effective agitation methods, accelerating fibril formation considerably. Although understanding the mechanisms of fibril formation is useful to treat amyloid-associated diseases, they are still unclear. Here, we performed several experiments of fibril formation altering ultrasonic amplitude and frequency. Considering the molecular mechanisms of ultrasonication-dependent fibril formation, generation of the cavitation bubbles by ultrasonic irradiation of aqueous solution would play a central role. Ultrasonication induces the accumulation and conformation change of proteins and peptides on the surface of cavitation bubbles, increasing supersaturation level and thus breaking supersaturation. This approach will contribute to understanding the amyloidogenicity of various proteins and to the creation of therapeutic strategies against a wide range of degenerative diseases.

収録刊行物

• ソノケミストリー討論会講演論文集

  ソノケミストリー討論会講演論文集 23 (0), 13-14, 2014

  日本ソノケミストリー学会

キーワード

• amyloid
• ultrasonic amplitude
• cavitation bubbles
• high-throughput assay

詳細情報

• CRID: 1390001206051220608
• NII論文ID: 110010013659
• DOI: 10.20577/pamjss.23.0_13
• 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