Biological Effects of Electromagnetic Radiation

Pirogova, Elena; Vojisavljevic, Vuk; Ćosić, Irena

doi:10.5772/7878

Cited by 21 publications

(11 citation statements)

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“…It has been shown in previous research that all protein sequences with the common biological function have common frequency component, which is a specific feature for the observed function/interaction [1,5,9]. This characteristic frequency is related to the protein biological function as it was found in our previous investigations [1][2][3][5][6][7][8][9][10]. Furthermore, it was shown that the proteins and their targets have the same characteristic frequency in common.…”

Section: Resonant Recognition Model (Rrm)mentioning

confidence: 75%

“…The RRM is based on the representation of the protein primary structure as a numerical series by assigning to each amino acid a physical parameter value relevant to the protein's biological activity. Although a number of amino acid indices have been found to correlate in some ways with the biological activity of the whole protein, our investigations [6,7] have shown that the best correlation can be achieved with parameters which are related to the energy of delocalised electrons of each amino acid. These findings can be explained by the fact that the electrons delocalised, from the particular amino acid, have the strongest impact on the electronic distribution of the whole protein.…”

Section: Resonant Recognition Model (Rrm)mentioning

confidence: 82%

“…These findings can be explained by the fact that the electrons delocalised, from the particular amino acid, have the strongest impact on the electronic distribution of the whole protein. In our extended studies, the energy of the delocalised electrons (calculated as the electron-ion interaction pseudopotential (EIIP) [1,[5][6][7]) of each amino acid residue was used. The resulting numerical series then represents the distribution of the free electrons energies along the protein.…”

Section: Resonant Recognition Model (Rrm)mentioning

confidence: 99%

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Quantum Foundations of Resonant Recognition Model

et al. 2010

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Biomolecular recognition is an open scientific problem, which has been investigated in many theoretical and experimental aspects. In that sense, there are encouraging results within Resonant Recognition Model (RRM), based on the finding that there is a significant correlation between spectra of the numerical presentation of amino acids in the primary structure of proteins and their biological activity. It has been found through an extensive research that proteins with the same biological function have a common frequency in their numerical spectra. This frequency was found then to be a characteristic feature for protein biological function or interaction The RRM model proposes that the selectivity of protein interactions is based on resonant energy transfer between interacting biomolecules and that this energy, electromagnetic in its nature, is in the frequency range of 10 13 to 10 15 Hz, which incorporates infra-red (IR), visible and a small portion of the ultra-violet (UV) radiation. In this paper, the quantum mechanical basis of the RRM model will be investigated using the solution in the simplified framework of Hückel-like theory of molecular orbits.

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Section: Resonant Recognition Model (Rrm)mentioning

confidence: 75%

Section: Resonant Recognition Model (Rrm)mentioning

confidence: 82%

Section: Resonant Recognition Model (Rrm)mentioning

confidence: 99%

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Quantum Foundations of Resonant Recognition Model

et al. 2010

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“…Our previous studies demonstrated that all protein sequences with a common biological function have a common frequency component in the free energy distribution of electrons along the protein backbone. This characteristic frequency was shown to be related to a protein biological function [5,[23][24][25][26]. Moreover, it was shown that proteins and their targets share the same characteristic frequency.…”

Section: Introductionmentioning

confidence: 99%

In vitro evaluation of low-intensity light radiation on murine melanoma (B16F10) cells

Peidaee

Almansour

Pirogova

2015

Med Biol Eng Comput

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Changes in the energy state of biomolecules induced by electromagnetic radiation lead to changes in biological functions of irradiated biomolecules. Using the RRM approach, it was computationally predicted that far-infrared light irradiation in the range of 3500-6000 nm affects biological activity of proto-oncogene proteins. This in vitro study evaluates quantitatively and qualitatively the effects of selected far-infrared exposures in the computationally determined wavelengths on mouse melanoma B16F10 cells and Chinese hamster ovarian (CHO) cells by MTT (thiazolyl blue tetrazolium bromide) cell proliferation assay and confocal laser-scanning microscopy (CLSM). This paper also presents the findings obtained from irradiating B16F10 and CHO cells by the selected wavelengths in visible and near-infrared range. The MTT results show that far-infrared wavelength irradiation induces detrimental effect on cellular viability of B16F10 cells, while that of normal CHO cells is not affected considerably. Moreover, CLSM images demonstrate visible cellular detachment of cancer cells. The observed effects support the hypothesis that far-infrared light irradiation within the computationally determined wavelength range induces biological effect on cancer cells. From irradiation of selected visible and near-infrared wavelengths, no visible changes were detected in cellular viability of either normal or cancer cells.

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“…It follows, therefore, that no classical concept is able to explain the long-range molecular interactions that occur between protein molecules. Further, in three-dimensional analysis of proteins and their ligands, it can be seen that the couplings do not have a well-defined or selective spatial and electrostatic complementarity, as proposed by the "key-lock" model [8,9]. There is evidence, meanwhile, that biological processes can be induced or modulated by electromagnetic fields of characteristic frequencies, as with light in photosynthetic systems [10] or with the increase in the catalytic activity of some enzymes on being irradiated with electromagnetic fields [11,12].…”

Section: Vaccinesmentioning

confidence: 99%

The Use of Planar Electromagnetic Fields in Effective Vaccine Design

Cortés¹,

Coral²,

McLachlan³

et al. 2017

Vaccines

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Vaccines have not yet been able to address the combination of three major obstacles: molecular coupling failure between peptide and human leukocyte antigen protein (HLA-II) molecule, failure to activate T-cells, and the molecular polymorphism displayed by all pathogens. Planar electromagnetic fields found in protein systems may play a role in all three problems. These amino acid planes are universal, selective in nature, and able to generate long distance attraction toward their corresponding ligand. We propose three molecular mechanisms through which to engineer molecular pattern interaction toward the intelligent design of more effective vaccines.

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Biological Effects of Electromagnetic Radiation

Cited by 21 publications

References 0 publications

Quantum Foundations of Resonant Recognition Model

Quantum Foundations of Resonant Recognition Model

In vitro evaluation of low-intensity light radiation on murine melanoma (B16F10) cells

The Use of Planar Electromagnetic Fields in Effective Vaccine Design

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