Disrupting Dimeric β-Amyloid by Electric Fields

The early oligomers of the amyloid Aβ peptide are implicated in Alzheimer’s disease, but their transient nature complicates characterization structure and toxicity. Here, we investigate stability minimal toxic species, i.e., β-amyloid dimers, presence an oscillating electric field. We first use deep learning (AlphaFold-multimer) for generating initial models Aβ42 dimers. flexibility secondary content then analyzed by multiple runs molecular dynamics (MD). Structurally stable similar to ensemble representatives from microsecond-long MD sampling. Finally, employ validated model as starting simulations external field observe a fast decay β-sheet at high strengths. Control using helical dimer 42-residue leucine zipper show higher structural than dimer. simulation results provide evidence that (oscillating 1 GHz) can disrupt which should be further investigated experiments with brain organoids vitro eventually vivo.