Ultrasonication-dependent formation and degradation of α-synuclein amyloid fibrils.
Ultrasonication can be used to break the supersaturation of α-synuclein, a protein associated with Parkinson's disease, at pH7.4 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.
['Yagi|Hisashi|H|', 'Mizuno|Aiko|A|', 'So|Masatomo|M|', 'Hirano|Miki|M|', 'Adachi|Masayuki|M|', 'Akazawa-Ogawa|Yoko|Y|', 'Hagihara|Yoshihisa|Y|', 'Ikenoue|Tatsuya|T|', 'Lee|Young-Ho|YH|', 'Kawata|Yasushi|Y|', 'Goto|Yuji|Y|']
D000682:Amyloid D000818:Animals D002470:Cell Survival D004305:Dose-Response Relationship, Drug D004307:Dose-Response Relationship, Radiation D019220:High-Energy Shock Waves D016716:PC12 Cells D066329:Protein Aggregates D059748:Proteolysis D011829:Radiation Dosage D051381:Rats D013010:Sonication D051844:alpha-Synuclein
Supersaturation Parkinson's disease Amorphous aggregation Cytotoxicity Solubility Surface denaturation