The amyloid- beta (Aβ) protein is a peptide that plays a central role in the development and progression of Alzheimer's disease, originating from the cleavage of the amyloid precursor protein (APP). The peptide's structural variability is linked to different stages and manifestations of Alzheimer's pathology, making it a critical focus for understanding the disease. Current therapeutic strategies primarily involve pharmacological interventions, but they have met with limited success in altering the course of the disease. Our research introduces an innovative approach to address this challenge by employing electromagnetic waves, specifically at a frequency of 900 MHz We performed comprehensive electromagnetic simulations to explore the effects of this frequency on Aβ structures, aiming to offer an alternative non-invasive treatment avenue. Following these electromagnetic simulations, molecular dynamics (MD) simulations were carried out using the Large Scale Atomic/Molecular Massively Parallel Simulation (LAMMPS) software to further investigate the peptide’s response at the atomic and molecular level. These simulations provided insights into the structural dynamics of Aβ under electromagnetic influence, enabling a deeper understanding of the peptide’s behavior. To substantiate the findings from our simulations and the theoretical framework, we conducted a Thioflavin T (ThT) assay and western blot analysis on in vitro Aβ fibril samples which are treated with electromagnetic (EM) wave exposure using a TEM cell device. After 3 hours of EM wave exposure, a noticeable decrease in Aβ fibrils was observed. This experimental validation was essential in confirming the simulation results and reinforcing the theoretical basis of our approach. Together, simulations and experimental evidence provide a strong foundation for exploring electromagnetic-based treatments as a potential therapeutic intervention for Alzheimer’s disease.