Acceleration of amyloid fibril formation by multichannel sonochemical reactor

TL;DR

This paper introduces a multichannel ultrasound system that accelerates and controls amyloid fibril formation in proteins, improving reproducibility over traditional shaking methods for research and diagnostic applications.

Contribution

Development of a novel multichannel ultrasonic reactor with adjustable conditions for enhanced, reproducible amyloid fibril formation studies.

Findings

Ultrasound irradiation significantly accelerates amyloid fibril formation.

The system outperforms conventional shaking in speed and reproducibility.

Fibril formation acceleration is controllable via transducer voltage.

Abstract

Formation of amyloid fibrils of various amyloidogenic proteins is dramatically enhanced by ultrasound irradiation. For applying this phenomenon to the study of protein aggregation science and diagnosis of neurodegenerative diseases, a multichannel ultrasound irradiation system with individually adjustable ultrasound-irradiation conditions is necessary. Here, we develop a sonochemical reaction system, where an ultrasonic transducer is placed in each well of a 96-well microplate to perform ultrasonic irradiation of sample solutions under various conditions with high reproducibility, and applied it for studying amyloid-fibril formation of amyloid $\beta$, $\alpha$-synuclein, $\beta$2-microglobulin, and lysozyme. The results clearly show that our instrument is superior to conventional shaking method in terms of degree of acceleration and reproducibility of fibril formation reaction. The acceleration degree is controllable by controlling the driving voltage applied to each transducer. We have thus succeeded in developing a useful tool for the study of amyloid fibril formation in various proteins.