Ultrasonication: An Efficient Agitation for Accelerating the Supersaturation-Limited Amyloid Fibrillation of Proteins

Amyloid fibrils are self-assemblies of proteins with an ordered cross-β architecture. Because they are associated with serious disorders, understanding their structure and mechanism of fibrillation is important. Irradiation with ultrasonication leads to fragmentation of amyloid fibrils, useful for seeding experiments. Recently, ultrasonication has been found to trigger the spontaneous formation of fibrils in solutions of monomeric amyloidogenic proteins. The results indicate that amyloid fibrillation is similar to the crystallization of solutes from a supersaturated solution. The accelerating effects of ultrasonication on amyloid fibrillation suggest that cavitation microbubbles play a key role in effectively converting the metastable state of supersaturation to the labile state, leading to spontaneous fibrillation. Moreover, ultrasonic irradiation would be promising for a high-throughput screening assay of amyloid fibrillation, advancing the study of supersaturation-limited amyloidogenesis.