Abstract
The phenomenon of knotted electromagnetic field (KEMF) is now actively studied, as such fields are characterized by a nontrivial topology. The research in this field is mainly aimed at technical applications – for instance, the development of efficient communication systems. Until present, however, the influence of KEMF on biological objects (including enzyme systems) was not considered. Herein, we have studied the influence of KEMF on the aggregation and enzymatic activity of a protein with the example of horseradish peroxidase (HRP). The test HRP solution was irradiated in KEMF (the radiation power density was 10−12 W/cm2 at 2.3 GHz frequency) for 40 min. After the irradiation, the aggregation of HRP was examined by atomic force microscopy (AFM) at the single-molecule level. The enzymatic activity was monitored by conventional spectrophotometry. It has been demonstrated that an increased aggregation of HRP, adsorbed on the AFM substrate surface, was observed after irradiation of the protein sample in KEMF with low (10−12 W/cm2) radiation power density; at the same time, the enzymatic activity remained unchanged. The results obtained herein can be used in the development of models describing the interaction of enzymes with electromagnetic field. The obtained data can also be of importance considering possible pathological factors that can take place upon the influence of KEMF on biological objects— for instance, changes in hemodynamics due to increased protein aggregation are possible; the functionality of protein complexes can also be affected by aggregation of their protein subunits. These effects should also be taken into account in the development of novel highly sensitive systems for human serological diagnostics of breast cancer, prostate cancer, brain cancer and other oncological pathologies, and for diagnostics of diseases in animals, and crops.
Highlights
It is known that electromagnetic radiation of various intensity can have different influence on human body
The level of background radiation within a typical radiometer bandwidth (~0.1 GHz) at a temperature of 310 К makes up 4 × 10−13 W13, while pathologies in human body are accompanied by radiation in the same frequency range at a level corresponding to a change in the brightness temperature of the order of 0.4 °С13
In our present work, we have studied the influence of knotted electromagnetic field (KEMF) with 2.3 GHz frequency and a power density of 10−12W/cm[2] on an enzyme protein
Summary
It is known that electromagnetic radiation of various intensity can have different influence on human body. The level of background radiation within a typical radiometer bandwidth (~0.1 GHz) at a temperature of 310 К makes up 4 × 10−13 W13, while pathologies in human body are accompanied by radiation in the same frequency range at a level corresponding to a change in the brightness temperature of the order of 0.4 °С13 In this connection, studies on the influence of electromagnetic radiation in these low-level ranges of power and frequencies on biological objects seem to be relevant. It is to be noted that, if the change in the structure does not affect the active site or chromophore groups of the enzyme, it is difficult to reveal such a change by monitoring the kinetic parameters of the catalysis reaction For this reason, in our present research, atomic force microscopy (AFM) has been employed for studying the influence of electromagnetic field on the HRP aggregation. The enzymatic activity of HRP in solution has been determined by spectrophotometry
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