Study type: 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.

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

Exposure

Exposure Parameters
Exposure 1: 50 Hz
Exposure duration: continuous for 3 h

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
Exposure duration continuous for 3 h
Exposure setup
Exposure source
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:

Methods Endpoint/measurement parameters/methodology

Investigated system:
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:

Study funded by

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