2015年
Ultrasonication-dependent formation and degradation of α-synuclein amyloid fibrils
Biochimica et Biophysica Acta - Biomembranes
- 巻
- 1854
- 号
- 1
- 開始ページ
- 209
- 終了ページ
- 217
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1016/j.bbapap.2014.12.014
- 出版者・発行元
- Elsevier
Ultrasonication can be used to break the supersaturation of α-synuclein, a protein associated with Parkinson's disease, at pH 7.4 above the critical concentration of fibrillation, thereby inducing the formation of amyloid fibrils. We speculated that ultrasonication could also be used to depolymerize preformed fibrils below the critical concentration. However, extensive ultrasonic irradiation transformed preformed fibrils into amorphous aggregates even above the critical concentration. Exposing preformed fibrils to the hydrophobic air-water interface of cavitation bubbles may have destabilized the fibrils and stabilized amorphous aggregates. Upon extensive ultrasonic irradiation, the accompanying decomposition of chemical structures was suggested when monitored by analytical ultracentrifugation. Amorphous aggregates produced by extensive ultrasonication showed higher cytotoxicity, suggesting that, although ultrasonication might be a useful approach for inactivating amyloid fibrils, potential cytotoxicity of amorphous aggregates should be considered.
- リンク情報
- ID情報
-
- DOI : 10.1016/j.bbapap.2014.12.014
- ISSN : 1879-2642
- ISSN : 0005-2736
- PubMed ID : 25528988
- SCOPUS ID : 84937111769