Mechanisms of Ultrasonically Induced Fibrillation of Amyloid β<sub>1–40</sub> Peptides

書誌事項

タイトル別名
  • Mechanisms of ultrasonically induced fibrillation of amyloid β₁₋₄₀ peptides
  • Mechanisms of ultrasonically induced fibrillation of amyloid β1-40 peptides

この論文をさがす

抄録

Kentaro Uesugi, Hirotsugu Ogi, Masahiko Fukushima, Masatomo So, Hisashi Yagi, Yuji Goto and Masahiko Hirao. Mechanisms of ultrasonically induced fibrillation of amyloid β₁₋₄₀ peptides. Japanese Journal of Applied Physics, 52(7S), 07HE10. https://doi.org/10.7567/JJAP.52.07HE10.

We systematically study the relationship between the ultrasonically induced aggregation behavior of amyloid β₁₋₄₀ peptide and acoustic pressures to clarify the dominant mechanism of the aggregation. With ultrasonic irradiation, the thioflavin-T (ThT) level of the A solution rises after a lag time, takes a maximum at 5 h, and remains unchanged or decreases. Thus, we monitor the ThT level at 5 h to evaluate the progress of the β-sheet structure and investigate its correlation with the acoustic pressures of fundamental and harmonics waves. The second-harmonics-wave amplitude shows the highest correlation with the ThT level, indicating the dominant contribution of cavitation bubbles to the fibrillation phenomenon. The influence of solution pH and Ar gas are investigated to identify the aggregation mechanism. As a result, local condensation of the peptide due to the high affinity of hydrophobic residues to the bubble-solution interface causes a highly supersaturated solution, leading to precipitation of β-sheet-rich nuclei.

収録刊行物

被引用文献 (5)*注記

もっと見る

参考文献 (39)*注記

もっと見る

関連プロジェクト

もっと見る

詳細情報 詳細情報について

問題の指摘

ページトップへ