Department of Physics, University of Messina, Messina, Italy.
J Phys Chem B. 2010 Sep 23;114(37):12144-9. doi: 10.1021/jp104226p.
The effects of extremely low frequency electromagnetic field on the protein structure of hemoglobin were investigated by means of Fourier transform infrared spectroscopy. Three samples of different hemoglobin aqueous solutions (also in the presence of sucrose and trehalose) were exposed to a 50 Hz electromagnetic field at 1 mT, and FTIR measurements were performed after 3 h of exposure. Quantitative spectral analysis revealed an evident decrease in amide A band intensity for hemoglobin in bidistilled water and sucrose aqueous solutions, but not for hemoglobin in trehalose aqueous solution. In addition a low relative increase of β-sheet in amide I region was detected for hemoglobin in both bidistilled water and sucrose aqueous solutions, whereas no appreciable changes were evidenced in the infrared spectra of hemoglobin in trehalose aqueous solutions. These results led us to conclude that a 50 Hz electromagnetic field can affect the N-H plane bending and C-N stretching vibrations of peptide linkages, suggesting compensatory mechanisms by means of environmental biochemical agents, such as evidenced by a protective effect of trehalose toward a low-frequency electromagnetic field.
采用傅里叶变换红外光谱法研究了极低频电磁场对血红蛋白蛋白质结构的影响。将三种不同的血红蛋白水溶液样品（也存在蔗糖和海藻糖）暴露于 1 mT 的 50 Hz 电磁场中，并在暴露 3 小时后进行 FTIR 测量。定量光谱分析表明，双蒸馏水和蔗糖水溶液中血红蛋白的酰胺 A 带强度明显降低，但海藻糖水溶液中血红蛋白的酰胺 A 带强度没有降低。此外，还检测到双蒸馏水和蔗糖水溶液中血红蛋白的酰胺 I 区β-折叠的相对增加较低，而在海藻糖水溶液中血红蛋白的红外光谱中没有明显变化。这些结果表明，50 Hz 电磁场可以影响肽键的 N-H 面弯曲和 C-N 伸缩振动，表明通过环境生化剂存在补偿机制，如海藻糖对低频电磁场的保护作用所证明的那样。
