Studying the electromagnetic-induced changes of the secondary structure of bovine serum albumin and the bioprotective effectiveness of trehalose by Fourier transform infrared spectroscopy.

Samples of bovine serum albumin in H(2)O and D(2)O solutions, in the absence or presence of trehalose, were exposed separately to a static magnetic field at 200 mT and to a 50 Hz electromagnetic field at 1.8 mT, studying the relative effects on the secondary structure of the protein by means of Fourier transform infrared spectroscopy. The spectra acquired in the mid-infrared region after 2 and 4 h of exposures to the static magnetic field showed a decrease in amide A and amide I band intensities for the protein in bidistilled aqueous solutions that was also evidenced after exposures to a 50 Hz electromagnetic field. These results led us to conclude that electromagnetic fields of low intensities can affect the C═O and C-N stretching vibrations and N-H plane bending of peptide linkages. Furthermore, mid-infrared spectra of bovine serum albumin in trehalose aqueous solutions were not significantly modified after the exposures, confirming the hypothesis of the possible bioprotective effectiveness of trehalose against electromagnetic fields.