Molecular mechanisms associated with the interaction of external electromagnetic fields in protein dynamics and aggregation: a focus on amyloid-βpeptide.

Transcranial stimulation has emerged as a non-invasive treatment that applies electrical currents and magnetic fields to regulate brain functions. Previous studies have shown that magnetic stimulation modulates the dynamics of charged molecules in biological systems. In some pathologies, once the electrical or magnetic field is applied directly to subjects, it can interact with, and alter, abnormally folded proteins, including amyloid-βpeptides and their aggregates, reducing cognitive impairments. While our understanding of the molecular mechanisms underlying the interaction between amyloid-βpeptide and the physical forces generated by electrical or magnetic stimulation remains unclear, observations show that these stimuli exert attractive and repulsive forces while interacting with the charged groups of peptide side chains as well as lipids. These interactions influence hydrophobic packing and secondary structure, ultimately inducing alterations in aggregation kinetics. The study of structural models of amyloidogenic proteins aids in understanding the mechanisms involved in the protein aggregation process and suggests possible therapeutic applications. This review examines proposed molecular mechanisms to explain the modulatory effects of external electromagnetic fields on the dynamics of proteins and their complexes that regulate pathological processes associated with amyloid-βpeptide fibrillation.