Vojisavljevic Vuk, Pirogova Elena, Cosic Irena
Royal Melbourne Institute of Technology, SECE, Melbourne, Victoria, Australia.
Int J Radiat Biol. 2007 Apr;83(4):221-30. doi: 10.1080/09553000701227565.
This work is based on our earlier research of the Resonant Recognition Model (RRM), where we have proposed that protein activation is electromagnetic in its nature. In this study we investigated experimentally the possibility of modulating the protein activity by the electromagnetic radiation of the specific frequency. The concept is studied here by applying a visible light radiation to example of 1-Lactate Dehydrogenase enzyme (LDH).
The selected LDH example is radiated by monochromatic visible light in a frequency range predicted computationally by the RRM. The kinetics of the irradiated LDH is measured by continuous monitoring of the NADH absorption at 340 nm.
A comparative analysis of the LDH enzyme activity before and after the electromagnetic field (EMF) exposures is performed. It was found that the LDH activity is selectively increased only by the radiation at the particular wavelengths of 595 nm and 828 nm. These experimentally determined wavelengths of the applied EMF are within the range predicted by the RRM.
Results reveal the LDH activity was modulated by the EMF exposures at the computationally predicted frequencies. The RRM concept presented provides new insights into proteins susceptibility to perturbation by electromagnetic radiation and possibility to program, predict, design and modify proteins and their bioactivity.
本研究基于我们早期对共振识别模型（RRM）的研究，我们在该研究中提出蛋白质激活本质上是电磁性的。在本研究中，我们通过实验研究了利用特定频率的电磁辐射调节蛋白质活性的可能性。这里通过以1-乳酸脱氢酶（LDH）为例应用可见光辐射来研究这一概念。
所选的LDH样本在RRM通过计算预测的频率范围内用单色可见光进行辐射。通过连续监测340nm处NADH的吸光度来测量辐照后LDH的动力学。
对电磁场（EMF）暴露前后的LDH酶活性进行了比较分析。发现仅在595nm和828nm的特定波长处的辐射会选择性地增加LDH活性。这些通过实验确定的所施加EMF的波长在RRM预测的范围内。
结果表明，在通过计算预测的频率下，EMF暴露可调节LDH活性。所提出的RRM概念为蛋白质对电磁辐射扰动的敏感性以及对蛋白质及其生物活性进行编程、预测、设计和修饰的可能性提供了新的见解。
