MISC

査読有り
2014年4月

超音波による蛋白質のアミロイド形成・結晶化の促進

生物物理
  • 宗 正智
  • ,
  • 八木 寿梓
  • ,
  • 後藤 祐児

54
6
開始ページ
297
終了ページ
302
記述言語
日本語
掲載種別
記事・総説・解説・論説等(学術雑誌)
出版者・発行元
The Biophysical Society of Japan General Incorporated Association

Protein crystals form in supersaturated solutions via a nucleation and growth mechanism. The amyloid fibrils of denatured proteins also form via a nucleation and growth mechanism. This similarity suggests that, although protein crystals and amyloid fibrils are distinct in their morphologies, both processes can be controlled in a similar manner. We show that ultrasonication is one of the most effective methods of agitation for accelerating spontaneous fibrillation. We also show that ultrasonication is also useful for forming crystals of proteins. We address the underlying mechanism of the ultrasonication-dependent breakdown of supersaturation, leading to the formation of amyloid fibrils or protein crystals.

リンク情報
URL
http://ci.nii.ac.jp/naid/130004713028

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