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Advances in Physical ChemistryVolume 2012 2012, Article ID 970369, 6 pages

Research ArticleDepartment of Physics, University of Messina, Street D’Alcontres 31, 98166 Messina, Italy

Received 8 April 2012; Revised 1 July 2012; Accepted 23 July 2012

Academic Editor: Sergei Tretiak

Copyright © 2012 Emanuele Calabrò and Salvatore Magazù. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

FTIR spectroscopy was used to investigate the effects of extremely low frequency 50 Hz electromagnetic field and of microwaves at 900 MHz on the secondary structure of a typical protein, the lysozyme, evaluating the bioprotective effectiveness of trehalose. Lysozyme in D2O solution 60 mg-ml was exposed to 50 Hz frequency electromagnetic field at 180 μT. The FTIR spectra indicated an increase of CH2 group at 1921 and 1853 cm

after 3 h of exposure. Such effect was not observed after the addition of trehalose 150 mg-mL at the same exposure conditions. Lysozyme dissolved in D2O at the concentration of 100 mg-mL was exposed up to 4 h to 900 MHz mobile phone microwaves at 25 mA-m. A significant increase in intensity of the amide I vibration band in the secondary structure of the protein was observed after 4 h exposure to microwaves. This effect was inhibited by the presence of trehalose at the concentration of 150 mg-mL. Fourier self-deconvolution spectral analysis of lysozyme in D2O solution after exposure to microwaves revealed an increase in intensity of the conformational components of amide I mode, particularly of β-sheet and turn that can be attributed to disorder and unfolding processes of the protein.





Autor: Emanuele Calabrò and Salvatore Magazù

Fuente: https://www.hindawi.com/



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