Medical/biological study (experimental study)

FTIR spectroscopy studies on the bioprotective effectiveness of trehalose on human hemoglobin aqueous solutions under 50 Hz electromagnetic field exposure med./bio.

By: Magazu S, Calabro E, Campo S

Published in: J Phys Chem B 2010; 114 (37): 12144-12149

Aim of study (acc. to author)

To study the effects of an extremely low frequency electromagnetic field on the protein structure of hemoglobin and the bioprotective effectiveness of two disaccharides.

Background/further details

Three samples of different hemoglobin aqueous solutions (from ten healthy donors) were exposed to a 50 Hz electromagnetic field (also with 50 mg/ml sucrose or trehalose) and measurements were performed after 3 h of exposure.
Proteins exist in different structures (e.g. beta-sheet and alpha-helix structure are typical secondary protein structures) generating different vibration bands within the FTIR spectroscopy (an infrared spectroscopy). Different amide bands originating from vibrations of the peptide or protein backbone are characteristic for protein vibration spectra.

Endpoint

structure of haemoglobin

Exposure

Exposure	Parameters
Exposure 1: 50 Hz Exposure duration: continuous for 3 h	magnetic flux density: 1 mT

General information

Hemoglobin was investigated i) in aqueous solution ii) in the presence of sucrose iii) in the presence of trehalose

Exposure 1

Main characteristics

Frequency	50 Hz
Type	magnetic field
Exposure duration	continuous for 3 h

Exposure setup

Exposure source	Helmholtz coils
Setup	couple of Helmholtz coils; uniform field at the center of the coil distance, where the samples were placed
Sham exposure	A sham exposure was conducted.

Parameters

Measurand	Value	Type	Method	Mass	Remarks
magnetic flux density	1 mT	-	measured	-	-

Exposed system:

isolated bio./chem. substance
aqueous haemoglobin solution

Methods Endpoint/measurement parameters/methodology

structure of haemoglobin (intensity of different vibration bands of protein linkages; quantitative spectral analysis; FTIR spectroscopy)

Investigated system:

isolated bio./chem. substance
aqueous haemoglobin solution

Time of investigation:

after exposure

Main outcome of study (acc. to author)

The extremely low frequency electromagnetic field exposure affected infrared vibration bands of hemoglobin. Some changes, such as the relative increase in beta-sheet with respect to alpha-helix content in the amide I region, appeared barely perceptible, whereas an evident decrease in the intensity of the amide A band was observed after 3 h of exposure for haemoglobin in both water and aqueous sucrose solutions. In contrast, extremely low frequency electromagnetic fields did not affect the infrared spectrum of hemoglobin in trehalose solution, supporting the hypothesis of possible protective effects of disaccharides such as trehalose against extremely low frequency electromagnetic fields.

Study character:

medical/biological study
experimental study
full/main study

Study funded by

not stated/no funding

Calabro E (2016): Competition between hydrogen bonding and protein aggregation in neuronal-like cells under exposure to 50 Hz magnetic field
Magazu S et al. (2011): Studying the Electromagnetic-Induced Changes of the Secondary Structure of Bovine Serum Albumin and the Bioprotective Effectiveness of Trehalose by Fourier Transform Infrared Spectroscopy
Calabro E et al. (2011): Static and 50 Hz Electromagnetic Fields Effects on Human Neuronal-Like Cells Vibration Bands in the Mid-Infrared Region
Mousavy SJ et al. (2009): Effects of mobile phone radiofrequency on the structure and function of the normal human hemoglobin
Giuliani L et al. (2008): Action of combined magnetic fields on aqueous solution of glutamic acid: the further development of investigations
Cleary SF et al. (1985): Erythrocyte hemolysis by radiofrequency fields