High-frequency terahertz waves disrupt Alzheimer’s β-amyloid fibril formation

Abstract

The accumulation and deposition of amyloid can cause a variety of neurodegenerative diseases, including Alzheimer’s and Parkinson’s disease. The degradation or clearance of this accumulation is currently the most widely accepted therapeutic strategy for intervention in these pathologies. Our study on amyloid-β (Aβ) oligomers in vitro revealed that high-frequency terahertz (THz) waves at a specific frequency of 34.88 THz could serve as a physical, efficient, non-thermal denaturation technique to delay the fibrotic process by 80%, as monitored by a thioflavine T (ThT) binding assay and Fourier transform infrared (FTIR) spectroscopy. Additionally, THz waves of this frequency have been shown to have no side effects on normal cells, as confirmed by cell viability and mitochondrial membrane potential assays. Furthermore, molecular dynamic (MD) simulations revealed that the THz waves could resonate with Aβ fibrils, disrupting the dense conformation by breaking the β-sheet structure and promoting the formation of abundant coil and bend structures. This study uses the amyloid of Aβ as an example, and the results will further guide interventions for the accumulation of other amyloids, which may provide new ideas for the remission of related diseases.