Fourier Self-Deconvolution Analysis of β-Sheet Contents in the Amide I Region of Hemoglobin Aqueous Solutions under Exposure to 900 MHz Microwaves and Bioprotective Effectiveness of Sugar and Salt Solutions

Abstract

Spectroscopic Fourier self-deconvolution analysis was used to investigate β-sheet features in the secondary structure of hemoglobin under mobile phone microwaves at 900 MHz. To this end, four samples of hemoglobin in bidistilled water, sucrose, trehalose, and sodium chloride aqueous solutions were exposed for up to 4 hr to 900 MHz microwaves at an average H-field intensity of 42 mA/m. Quantitative spectral analyses highlighted significant increases in β-sheet contents in the Amide I region of hemoglobin samples in bidistilled water solution, but no appreciable change was observed in hemoglobin samples in sucrose, trehalose, and sodium chloride solutions. These results led us to conclude that mobile phone microwaves can denaturate hemoglobin in bidistilled water solution whereas sucrose, trehalose, and sodium chloride solutions produce a protective effect against microwaves, preserving the protein from unfolding.