Frequency-Dependent Effects of a 26 GHz Electric Field on SOD1 Dynamics: Molecular Dynamics Simulations

Cu/Zn superoxide dismutase 1 (SOD1) is a key antioxidant enzyme that regulates cellular redox balance by catalysing the dismutation of superoxide radicals into molecular oxygen and hydrogen peroxide. The catalytic activity of SOD1 is strongly influenced by its surrounding electrostatic environment, making it a suitable model to explore potential non-thermal effects induced by external electric fields. Previous investigations employing continuous wave electric fields have suggested that SOD1 exhibits a frequency-specific response, while more recent computational studies using nanosecond pulsed electric fields (nsPEFs) have reported measurable modulations on SOD1 without detecting protein unfolding. Building on these findings, the present work relies on all-atom molecular dynamics (MD) simulations to assess the effects of a 26 GHz radiofrequency (RF) electric field on SOD1, using a static electric field as a benchmark reference. Comparative analyses exhibit enhanced conformational fluctuations under 26 GHz exposure, whereas the reference condition shows only minor deviations from control. Although subtle and below the unfolding threshold, these effects delineate a differential protein response to timevarying and static electric fields and motivate further investigations into field-protein coupling mechanisms at the molecular level.