Mechanisms of Ultrasonically Induced Fibrillation of Amyloid β<sub>1–40</sub> Peptides
書誌事項
- タイトル別名
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- Mechanisms of ultrasonically induced fibrillation of amyloid β₁₋₄₀ peptides
- Mechanisms of ultrasonically induced fibrillation of amyloid β1-40 peptides
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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
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- Japanese Journal of Applied Physics
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Japanese Journal of Applied Physics 52 07HE10-, 2013-06-20
The Japan Society of Applied Physics
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詳細情報 詳細情報について
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- CRID
- 1050581168900568960
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- NII論文ID
- 120007148369
- 40019765024
- 210000142516
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- NII書誌ID
- AA12295836
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- ISSN
- 13474065
- 00214922
- http://id.crossref.org/issn/13474065
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- HANDLE
- 11094/84169
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- NDL書誌ID
- 024799623
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- 本文言語コード
- en
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- 資料種別
- journal article
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- データソース種別
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- IRDB
- NDL
- Crossref
- CiNii Articles
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