CHARACTERIZING ALTERATIONS IN THE SECONDARY STRUCTURE OF TYPICAL PROTEINS UNDER EXPOSURE TO ELECTROMAGNETIC FIELDS

Emanuele Calabrò (1, 2, 3) , Salvatore Magazù (4, 5, 6, 7)

1 Physical Sciences and Earth Sciences of Messina University [Messina, Italy]
2 CISFA - Interuniversity Consortium of Applied Physical Sciences [Messina, Italy]
3 Industrial Technical Institute “Verona Trento-Majorana-Marconi [Messina, Italy]
4 CBM - Centre de biophysique moléculaire
5 LE STUDIUM - LE STUDIUM
6 ICMN - Interfaces, Confinement, Matériaux et Nanostructures
7 INdAM Unit - Istituto Nazionale di Alta Matematica "Francesco Severi" [Roma]

Over the past decades, the growing demand for electric power, electronic devices and radio frequency patterns has induced human beings to use low- and high-frequency electromagnetic fields. Nevertheless, previous research has shown that exposure to electromagnetic fields can induce health effects in living organisms. In particular, several epidemiological studies have reported a correlation between an increased risk of cancer and exposure to extremely lowfrequency electromagnetic fields. Also, in vitro tests have demonstrated that radio frequencies and microwaves emitted by mobile phones and other electronic devices can be carcinogenic and cause DNA damage and chromosome aberrations. In order to investigate accurately the alterations in living things induced by electromagnetic fields, the effects of exposure of typical proteins to low-frequency electromagnetic fields and to microwaves have been studied. Indeed, proteins are fundamental in the organic metabolism of living creatures and it has been clearly demonstrated that several types of environmental stress agents can alter the secondary structure of proteins. To this aim, Fourier Transform Infrared (FTIR) Spectroscopy was used to investigate the structure of proteins in a water solution, because it may be considered the most versatile spectroscopic technique for analyzing the secondary structure of a protein in various physiochemical environments. In fact, infrared spectroscopy detects transitions between rotational and vibration energy levels, yielding much more information on molecular structure, in particular on proteins. FTIR spectroscopy analysis showed that exposure to electromagnetic fields at intensities below the levels recommended by the International Commission on Non-Ionizing Radiation Protection, alters the secondary structure of typical proteins such as hemoglobin, myoglobin, bovine serum albumin and lysozyme. In particular, it was shown that exposure to electromagnetic fields induces the unfolding of proteins represented by transitions from the α-helix to the β-sheet structure, which may be responsible for the aggregation phenomena. Protein aggregation can lead to neurotoxic and neurodegenerative disorders that are the precursors of some pathologies.

Domaines: Chimie

Emanuele Calabrò, Salvatore Magazù. CHARACTERIZING ALTERATIONS IN THE SECONDARY STRUCTURE OF TYPICAL PROTEINS UNDER EXPOSURE TO ELECTROMAGNETIC FIELDS. Advances in Chemistry Research, 42, 2018, : 978-1-53612-919-9. ⟨hal-02557287⟩