Spectroscopic investigation of tau protein conformational changes by static magnetic field exposure

Abstract

Electromagnetic fields taint the molecular environment of proteins and induce changes in the central nervous system. This research applied Fourier transform infrared spectroscopic analysis to investigate the effects of static magnetic fields on tau protein in neurological disorders. It explores the conformational changes of tau protein and highlights its’ potential application as a pathological biomarker for early detection and therapeutic interventions. The results indicate that tau protein is susceptible to magnetic field exposure in the amide B, fingerprint, and amide regions (IV-VI). Changes in peak positions and band intensities were identified and delineated as the outcome effect of magnetic forces on molecular vibrations. Magnetic forces may affect the microtubule structure of the tau protein, leading to protein aggregation. These results indicate the potential application of FTIR spectroscopy for the early detection and classification of degenerative diseases through spectrum analysis. Different magnetic fields can be used as spontaneous therapeutic procedures to induce changes in the molecular environment of proteins.