A13 超音波による蛋白質溶液の過飽和状態の解消

• 後藤 祐児

  阪大蛋白研

書誌事項

タイトル別名

• A13 Ultrasonication-dependent breakdown of protein supersaturations

抄録

Amyloid fibrils are associated with various diseases such as Alzheimer's disease and type II diabetes. Amyloid fibril formation consists of nucleation and growth. The nucleation process does not readily occur. Once the nucleus formed, however, subsequent growth proceeds rapidly. These characteristics of amyloid fibril formation are similar to those of the crystal growth of substances, where agitation of solution often accelerates the nucleation process. We found that ultrasonication is useful for inducing amyloid nucleation and thus the formation of fibrils. In other words, ultrasonication is effective in breaking the supersaturation of amyloidogenic proteins. This is likely true for crystallization of the native state of proteins. Taking advantage of the effects of ultrasonication, we develop several methodologies by which we monitor the supersaturation of protein solutions. Proteins also form amorphous aggregates distinct from ordered amyloid fibrils. We show that ultrasonication is also useful for distinguishing amorphous aggregates and 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

• 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 21 (0), 83-84, 2012

  日本ソノケミストリー学会

キーワード

• protein
• amyloid
• solubility
• supersaturation
• plate reader

詳細情報

• CRID: 1390282681028730880
• NII論文ID: 110009710749
• DOI: 10.20577/pamjss.21.0_83
• 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