抄録
Amyloid fibrils are highly ordered assemblies of misfolded proteins associated with over 30 degenerative diseases including Alzheimer’s diseases or type 2 diabetes. Fibrils, similar to crystals, form through nucleation and growth in a supersaturated solution. Fibril formation takes a long time because of the high free-energy barrier of nucleation. Ultrasonic irradiation is one of the most effective agitation methods, accelerating fibril formation considerably. Although understanding the mechanisms of fibril formation is useful to treat amyloid-associated diseases, they are still unclear. Here, we performed several experiments of ultrasonic irradiation of both monomeric protein solution and fibrils solution altering ultrasonic amplitude and frequency. Considering the molecular mechanisms of ultrasonication-dependent fibril formation, generation of the cavitation bubbles by ultrasonic irradiation of aqueous solution would play a central role. The generation of hydrophobic surface by ultrasonication leads to accumulation of proteins and alteration of their structure.
This approach will contribute to understanding the amyloidogenicity of various proteins and to the creation of therapeutic strategies against a wide range of degenerative diseases.
