The present review paper deals with experimental findings on the
shielding action effects of two homologous disaccharides, i.e. sucrose and trehalose,
against applied electromagnetic fields.
The study, performed by means of the Fourier Transform InfraRed technique, is
addressed to examine the effects of electromagnetic fields exposure on the secondary
structure of some prototypal proteins (haemoglobin, bovine serum albumin
and lysozyme) in aqueous solution, both in the absence and presence of the
More specifically, haemoglobin and bovine serum albumin water solutions, in the
absence and presence of sucrose and trehalose, were exposed to a uniform magnetic field of 200 mT.
The intensity of the amide A vibration band, for both haemoglobin and bovine serum albumin in bidistilled
water solution, drops down after three hours of exposure. The addition of sucrose and trehalose
reduces such a decrease.
Moreover, a three hours of exposure to a 50 Hz electromagnetic field at 1 mT of aqueous solutions
of haemoglobin causes a relative increase in intensity of the β-sheet component with respect to the
α-helix component in the amide I region; no appreciable spectral modifications were observed in
haemoglobin samples in the presence of trehalose or sucrose.
Finally, the effects of 1800 MHz microwaves on haemoglobin, bovine serum albumin and lysozyme
aqueous solutions were investigated under a 3 h exposure of a 21 mA/m H-field (average intensity).
FTIR analysis reveals a significant increase in intensity of proteins amide I and II modes after exposure,
but no appreciable changes are detected for haemoglobin in the presence of sucrose and trehalose,
confirming the hypothesis that disaccharides preserve proteins from electromagnetic fields.