The Shielding Action of Disaccharides for Typical Proteins in Aqueous Solution Against Static, 50 Hz and 1800 MHz Frequencies Electromagnetic Fields

Title:The Shielding Action of Disaccharides for Typical Proteins in Aqueous Solution Against Static, 50 Hz and 1800 MHz Frequencies Electromagnetic Fields

Volume: 10 Issue: 1

Author(s): Salvatore Magazù, Emanuele Calabro, Maria T. Caccamo and Antonio Cannuli

Affiliation:

Keywords: Electromagnetic field, Haemoglobin, Bovine Serum Albumin, Lysozyme, FTIR spectroscopy, trehalose, sucrose.

Abstract: 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 disaccharides.

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.

Cite this article as:

Magazù Salvatore, Calabro Emanuele, Caccamo T. Maria and Cannuli Antonio, The Shielding Action of Disaccharides for Typical Proteins in Aqueous Solution Against Static, 50 Hz and 1800 MHz Frequencies Electromagnetic Fields, Current Chemical Biology 2016; 10 (1) . https://dx.doi.org/10.2174/2212796810666160419153722