Calabrò Emanuele, Magazù Salvatore
Department of Mathematics and Informatics Sciences, Physics Sciences and Earth Sciences, University of Messina, Messina, Italy.
Bioelectromagnetics. 2017 Sep;38(6):447-455. doi: 10.1002/bem.22056. Epub 2017 Apr 28.
In this study, we report the effects of static magnetic fields (SMFs) at 200 mT on different hemoglobin aqueous solutions, in the absence and in the presence of sucrose and trehalose, studied by FTIR spectroscopic techniques. Significant decrease in intensity of Amide I and Amide II vibration bands was observed after 6 h exposure for hemoglobin in bidistilled water solution. Also, it was observed that the decrease in intensity of the Amide I band was larger than the Amide II after exposure. This result can be explained assuming that an SMF induces increase of hydrogen bonding in hemoglobin in bidistilled water solution. In particular, the use of second-derivative analysis highlighted two absorption peaks at 1907 and 2022 cm that can be attributed to nitrogen monoxide vibration and antisymmetric stretch of azide ion bound, respectively. These vibrations increased significantly after exposure to the SMF (P < 0.01). This result can be explained assuming that exposure to an SMF induces the orientation of nitrogen monoxide and azide ion ligands toward the direction of the field. Finally, it was observed that the addition of sucrose and trehalose in hemoglobin aqueous solution inhibited such alterations, suggesting that bioprotective effectiveness of these disaccharides occurs after exposure to an SMF. Bioelectromagnetics. 38:447-455, 2017. © 2017 Wiley Periodicals, Inc.
在本研究中，我们报告了通过傅里叶变换红外光谱技术研究的200 mT静磁场（SMF）对不同血红蛋白水溶液（有无蔗糖和海藻糖存在的情况下）的影响。在双蒸水溶液中，血红蛋白暴露6小时后，观察到酰胺I和酰胺II振动带的强度显著降低。此外，还观察到暴露后酰胺I带强度的降低大于酰胺II带。该结果可以通过假设SMF诱导双蒸水溶液中血红蛋白氢键增加来解释。特别是，二阶导数分析突出显示了在1907和2022 cm处的两个吸收峰，分别可归因于一氧化氮振动和结合的叠氮离子的反对称拉伸。暴露于SMF后，这些振动显著增加（P < 0.01）。该结果可以通过假设暴露于SMF会诱导一氧化氮和叠氮离子配体朝向磁场方向取向来解释。最后，观察到在血红蛋白水溶液中添加蔗糖和海藻糖可抑制此类变化，表明这些二糖的生物保护作用在暴露于SMF后发生。《生物电磁学》。38:447 - 455，2017年。© 2017威利期刊公司。
