H / D isotopic change effects on the secondary structure of bovine serum albumin under electromagnetic field exposure

A careful analysis of electromagnetic effects on the secondary structure of some proteins has been performed up to now [1-3]. Bovine serum albumin (BSA) is one of the most studied proteins utilized as a model for many and diverse biophysical and biochemical studies. A prominent spectral feature in the secondary structure of BSA is the amide A vibration in the IR spectra close to 3300 cm-1, which is due mostly to the peptide linkage N—H stretching mode. The effects of the exposure of BSA to a static magnetic field (SMF) at 200 mT and to a 50 Hz electromagnetic field (EMF) at 2 mT have been taken into account analyzing the changes of this vibration band by means of FTIR spectroscopy. It was observed that after 3 h of exposure, the intensity of the amide A vibration band decreased for BSA in bidistilled water solution exposed to the SMF and to the 50 Hz EMF (Fig.1-A and Fig. 1-C). The decreases in amide A intensity after analogue exposure of BSA in D2O solution were less than those detected in samples in bidistilled water solution, as can be observed in Fig.1-B and Fig.1-D.