Sound energy and amyloidogenic fibrillation

Structural proteins generate functionality in living systems as multimeric complexes that self-assemble with high precision to yield the machinery of life. A critical phenomenon in protein self-assembly is the formation of linear, nearly one-dimensional aggregates, characterized by continuous intermolecular beta-sheet connectivity. These structures are thermodynamically stable, even with respect to native folds in many cases, and the strength of the intermolecular bonding confers impressive mechanical properties. The structures, known generally as ‘amyloids’, are capable of autocatalytic growth in the presence of monomeric protein, and are pathognomonic for a range of serious diseases, such as Alzheimer’s disease. Aberrant fibrillar protein self-assembly is initiated at the molecular level by either partial or full disruption of a native protein fold, giving rise to new inter- and intramolecular interactions, and hence to the formation of protein fibrillar aggregates.

While the structural assembly of amyloid fibril at the atomistic and molecular level have been uncovered through a multiple of experimental and simulation-based studies, some of the aggregation modifying factors, such as sound energy, have been overlooked. The present research is focused on the effects of sound energy on the formation and breakage of intermolecular contacts in self-assembled protein amyloids.

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