title: Amyloid fibril disruption by ultrasonic cavitation: nonequilibrium molecular dynamics simulations.
abstract: We describe the disruption of amyloid fibrils of Alzheimer's amyloid-β peptides by ultrasonic cavitation. For this purpose, we performed nonequilibrium all-atom molecular dynamics simulations with sinusoidal pressure and visualized the process with movies. When the pressure is negative, a bubble is formed, usually at hydrophobic residues in the transmembrane region. Most β-strands maintain their secondary structures in the bubble. When the pressure becomes positive, the bubble collapses, and water molecules crash against the hydrophilic residues in the nontransmembrane region to disrupt the amyloid. Shorter amyloids require longer sonication times for disruption because they do not have enough hydrophobic residues to serve as a nucleus to form a bubble. These results agree with experiments in which monodispersed amyloid fibrils were obtained by ultrasonication.
authors.affiliation: Research Center for Computational Science, Institute for Molecular Science , Okazaki, Aichi 444-8585, Japan.
authors.forename: Hisashi
authors.initials: H
authors.lastname: Okumura
authors.forename: Satoru G
authors.initials: SG
authors.lastname: Itoh
mesh_terms: D000682:Amyloid / Q000737:chemistry / Q000648:ultrastructure*; D016229:Amyloid beta-Peptides / Q000737:chemistry / Q000648:ultrastructure; D006801:Humans; D056004:Molecular Dynamics Simulation; D017433:Protein Structure, Secondary; D013010:Sonication; D014465:Ultrasonics
chemical_list: D000682:Amyloid; D016229:Amyloid beta-Peptides