THE IR RANGE ELECTROMAGNETIC RADIATION OF NON-THERMAL INTENSITY AND THE “HORMESIS” PHENOMENON IN PROTEINS

I.V. Timofeyev, M.V. Kulak, A.A. Smetannikov, D.I. Timofeyev, S.I. Petrenko

Introduction

The “hormesis” phenomenon has received detailed coverage and was documented in various domains of science. Lately the term tends to be used to describe a pronounced physiological effect on a living organism in response to exposure to extra weak stimuli (S.V. Kaznacheyev, L.V. Molchanova, 1999).

We have observed “hormesis” in the protein molecules after exposure to low (0.7-0.8 mkm) and high (3-1000mkm) range IR electromagnetic radiation of non-thermal intensity. This phenomenon may be directly attributed to conformational change in protein, which in its turn may lead to changes in the protein function and exposure effect.

This is especially topical now when employment of highly effective chemical therapy preparations in particular antibiotics has been discredited due to continuous emergence of new strains of microorganisms possessing mono- or multiresistance to pharmaceuticals that once were considered efficacious. Hence it follows that research and development of innovative highly effective means for prevention and treatment of the most dangerous human maladies is a timely and topical challenge.

It is known with assurance that modified magnetic field provides an active factor capable of inducing metabolism changes in a living organism. (V.T. Podkovkin, L.S. Zotova, 2000). In connection with the above said the curing effect of exposure to a wide spectrum of electromagnetic fields and electromagnetic emissions comes into particular prominence. (V.P. Kaznacheyev, 1983; V.P. Kaznacheyev, L.P. Mikhailova, 1985).

The IR-therapy device “URO-BIOFON” is the apparatus capable of generating the IR range electromagnetic waves of non-thermal intensity (emission power below a thousandth fraction of a Watt) developed by experts from research and production enterprise “BIONIX” jointly with Izhevsk Machinery plant.

In this paper we study the effect of low-intensity electromagnetic radiation (LIEMR), generated by this device on the spectral characteristics of the model test-protein, dry and in solution.

Material and methods

The test was run with use of bovine serum albumine (BSA) for immunochemical reactions (produce of Belorussia). Weighing was carried out with the help of laboratory balance. The solutions were prepared in laboratory glassware by means of a magnetic mixer. The ready solutions were stored in a household freezer at –20oC. The optical density (OD) of the protein solutions was measured with Beckman DU-70 spectrophotometer in scanning mode.

The general protein determination was performed by the Biuret method. The prepared BCA weights were used to get the solutions of necessary concentration. Determination of the protein content in solution was carried out as follows: 0.2ml of Benedict’s reagent was added to 4ml of solution containing 0.1-2.0mg of protein dissolved in 3% NaOH solution. The solution was mixed thoroughly and photometered at 330nm wavelength. The protein content was determined by the standard protein curve.

Results

The LIEMR effect on the dry and dissolved model test-protein was studied by comparing the spectral characteristics obtained during scanning the protein solution in the visible and UV parts of the spectrum.

In the first series of experiments the 10mg weight of dry test-protein (BSA) was exposed to “URO-BIOFON” radiation (6 standard length cycles), after that a 0,1% BSA solution was prepared in 10ml of distilled water which was tested with the spectrophotometer in scanning mode. The same method was followed in preparing check samples (the native and the temperature treated ones) which then also were photometered but without prior exposure to LIEMR. The obtained results are shown in Table 1.

Table 1

As evident from the data of Table 1 above exposure of dry BSA to LIEMR from the “URO-BIOFON” device caused a drop in the protein optical density (OD 0.520) in the zone of maximal UV absorption peculiar for the protein molecules (l , -278-280nm) as compared to the check sample data. At the same time thermal denaturation of the protein sample by keeping it at +80°C leads to similar tendencies in the optical density change (0.469) and also in the UV absorption range characteristic of protein molecules. Besides the UV absorption peak wavelength shift was observed in both cases (from 226nm to 224nm). These data may be a demonstration of the changes taking place in the protein molecule structure as a result of exposure to LIEMR from “URO-BIOFON” and denaturation temperature. Similar OD change trends in the samples after electromagnetic and thermal exposure is testimony to possibly similar modifications in the spatial conformation of the model protein influenced by the abovesaid physical factors. It is important to note that one time freezing-thawing applied to the BSA solution samples (test and check) reveals ‘retention of the exposure effect’ and no significant OD changes in the absorption spectrum are observed. When the freeze-thaw procedure was applied to the powder protein samples the native protein sample responded with the OD changes similar to those observed after exposure to “URO-BIOFON” radiation. On the other hand the samples exposed to high temperature treatment (+80°Ñ) revealed OD rise (up to 0.704 at l-278) in the range characteristic of the protein absorption spectrum. The 48 hours long storage of the check and high temperature treated dry samples at +8°C led to disapearance of the earlier observed OD changes, while the LIEMR exposure sample retained the OD changes in the characteristic UV absorption zone.

During the second series of experiments the tested 0.1% solution was made out of the native BSA and the solution samples underwent one-time, three-times and six-times LIEMR exposure with subsequent examination of the spectral parameters in the visible and UV spectrum areas as compared against the check samples. The results are shown in Table 2.

Table 2

As shown in Table 2 the one-time LIEMR exposure of the 0.1% BSA solution caused change on the peak OD parameter of the protein ( at l -278 to 0.624) in the protein molecule characteristic range as compared against the OD of the check samples. Increase in the number of exposures did not lead to any significant OD or wavelength changes.

Conclusion

This provides an experimental demonstration of the effect that extraweak IR electromagnetic radiation of non-thermal intensity (0.7-1000mkm range) has on the properties of model protein.

It is common knowledge that biological effect of low-intensity EM radiation on the organism is implemented through the magnetically induced diffuse instability, i.e. the Postnikov-Maslovsky effect (M.V. Maslovsky et al, 2000). This instability may come to existence during rise in mobility of molecules and atoms and stems from rupture of links in protein molecules and their formations which determine the main structural and functional characteristics of biological systems. In turn the restructuring in molecular and supramolecular formations may lead to a new functional mode of the entire organism.

Since the LIEMR exposure effectiveness in our experiments with the test-protein did not depend on the number of exposures (1 to 6 exposures), this may be attributed to the above mentioned ‘hormesis’ phenomenon in the protein molecule, when a weak external signal causes hormesis thanks to an instantaneous rise of its magnitude due to resonance with the internal structure. It is obvious that this is the very moment (simultaneously with LIEMR from “URO-BIOFON”) when the conformapion changes in the structure of the tested BSA samples take place, peculiar for proteins in the UV part of the spectrum.

Taking into consideration the fact that life on Earth exists only in form of ‘protein structures’ it is safe to assume that low intensity electromagnetic fields and the observed hormesis in proteins are of vital importance.

List of reference

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