Magazù Salvatore, Calabrò Emanuele, Campo Salvatore, Interdonato Salvatore
Department of Physics, University of Messina, Viale Stagno D'Alcontres, 31-98166 Messina, Italy.
J Biol Phys. 2012 Jan;38(1):61-74. doi: 10.1007/s10867-010-9209-1. Epub 2011 Mar 9.
The aim of this study was the investigation of static magnetic field effects on haemoglobin secondary structure and the bioprotective effectiveness of two disaccharides, sucrose and trehalose. Samples of haemoglobin aqueous solutions, in the absence and in the presence of sucrose and trehalose, were exposed to a uniform magnetic field at 200 mT, which is the exposure limit established by the ICNIRP recommendation for occupational exposure. Spectral analysis by FTIR spectroscopy after 3 and 7 h of exposure revealed a decrease in the amide A vibration band for haemoglobin in bi-distilled water solution. Analogue exposures did not produce any appreciable change of amide A for haemoglobin in sucrose and trehalose solutions. Otherwise, no relative increase of [Formula: see text]-sheet contents in amide I and II regions was detected for haemoglobin aqueous solutions, leading us to exclude the hypothesis that static magnetic fields can induce the formation of aggregates in the protein. In addition, a decrease in CH(3) stretching linkages occurred for haemoglobin in bi-distilled water solution after exposure, which was not observed for haemoglobin in sucrose and trehalose aqueous solutions, providing further evidence of a bioprotective compensatory mechanism of such disaccharides.
本研究的目的是调查静磁场对血红蛋白二级结构的影响以及两种二糖(蔗糖和海藻糖)的生物保护效果。血红蛋白水溶液样本,在不存在以及存在蔗糖和海藻糖的情况下,暴露于200 mT的均匀磁场中,这是国际非电离辐射防护委员会(ICNIRP)针对职业暴露所规定的暴露限值。暴露3小时和7小时后通过傅里叶变换红外光谱(FTIR)进行光谱分析,结果显示双蒸水溶液中的血红蛋白的酰胺A振动带下降。类似的暴露对蔗糖和海藻糖溶液中的血红蛋白的酰胺A未产生任何明显变化。此外,未检测到血红蛋白水溶液在酰胺I和II区域的β-折叠含量有相对增加,这使我们排除了静磁场可诱导蛋白质中聚集体形成的假设。另外,暴露后双蒸水溶液中的血红蛋白的CH(3)伸缩键发生了下降,而蔗糖和海藻糖水溶 液中的血红蛋白未观察到这种情况,这为这类二糖的生物保护补偿机制提供了进一步证据。