Abstract

Bioprotective effects of deuterium oxide solution on proteins' secondary structure against extremely low frequencies electromagnetic fields

Author(s): Emanuele Calabro, Salvatore Magazu

The effects of separated exposures to a static magnetic field at 200 mT and to a 50 Hz electromagnetic field at 2 mT on the secondary structure of a typical protein, the bovine serumalbumin (BSA), inH2O water solution and in deuterium oxide (D2O) solution have been taken into account analyzing the changes of characteristic vibration bands by means of FTIR spectroscopy. It was observed that after 3 h of separated exposure to the static magnetic field and to 50Hz electromagnetic field, amideAand amide I vibration bands decreased in intensity for BSA samples in bidistilled H2O water solution. In contrast, no significant change was observed in amide I and amideAmodes after exposure of BSA in D2O solution. This result can be explained by the hypothesis, advanced by other authors with respect to other stress agents, that H/D isotopic exchange can strengthen the hydrogen bond interaction providing that D2O can protect the secondary structure of a protein against the effects of extremely low frequency electromagnetic fields.