Low-frequency magnetic radiation leads to the broadening of valent bonds in protein infrared spectra.

ABSTRACT

In recent years it has been discovered that a long-term exposure to low frequency magnetic fields leads to changes in activity of biological systems both in vivo and in vitro. Molecular mechanisms of this phenomenon are not clear. The present work uses infrared (IR) spectroscopy to study the effect of alternating magnetic field on a structural state of purified proteins. It was revealed that a 1-h exposure of aqueous solution of bovine serum albumin (BSA) and gluten isolated from wheat to 5.75Hz magnetic field with maximum amplitude of 25mTl resulted, respectively, in a ∼1.5- and 2-fold increase of the width of the band related to the vibrations of valent bonds in the range of 3500-2750cm(-1) (p<0.05). Unlike aqueous solutions, the desiccated BSA films did not exhibit any effect of magnetic field on parameters of IR-spectra. It is suggested, that low frequency magnetic fields induce the broadening of bands in IR spectra due to changes in structural organization of delocalized protein-bound water molecules thereby affecting macromolecules and related cell reactions.