Parallel β‐sheet vibration band increases with proteins dipole moment under exposure to 1765 MHz microwaves

Calabrò, Emanuele; Magazù, Salvatore

doi:10.1002/bem.21956

Cited by 22 publications

(13 citation statements)

References 43 publications

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“…In addition, patch clamp technique can be used for measuring ionic currents across cellular membrane channels of the tumor tissue as a function of the frequency of an applied electromagnetic field, so that the largest value of ionic current would be measured at the natural resonance frequency of tumor cells. Furthermore, the largest decrease in cellular transmembrane potential in a tumor cell should occur at the natural resonant frequency, following the results obtained in previous studies by the authors of this study [16,17].…”

Section: Discussionsupporting

confidence: 86%

“…Neuroblastoma cell line SH-SY5Y was purchased from American Type Culture Collections (ATCC) (Rockville, MD) and was used as a cell model in this study. Cells were differentiated following the protocol accurately described in the previous studies [16,17].…”

Section: Methodsmentioning

confidence: 99%

“…Cell cultures were treated following the protocol of [35,36] and subjected to infrared (IR) spectroscopic techniques by a FTIR spectrometer Vertex 80v of Bruker Optics. For each spectrum, 128 interferograms were collected with a spectral resolution of 4 cm -1 , following the technical procedure described previously [16,17].…”

Section: Methodsmentioning

confidence: 99%

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New Perspectives in the Treatment of Tumor Cells by Electromagnetic Radiation at Resonance Frequencies in Cellular Membrane Channels

Calabrò¹,

Magazù²

2019

TOBIOTJ

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Background: The use of electromagnetic fields has been considered as adjuvant therapy for the treatment of cancer given that some clinical trials have shown that the irradiation of cancer cells with electromagnetic fields can slow down the disease progression. Aims: We hypothesize that this effect could be amplified by irradiating tumor cells with electromagnetic fields having frequencies close to the natural resonant frequencies of membrane channels in tumor cells, in order to obtain a significant change of the ion flux across tumor cell membrane channels, inducing the largest harmful alteration in their cellular function. Methods: Neuronal-like cells were used as a cell model and exposed for 6 h to electromagnetic fields at different frequencies (0, 50 Hz, 900 MHz) at the same intensity of 2 mT. The exposure system was represented by two Helmholtz coils driven by a power amplifier in current mode and an arbitrary function generator. FTIR spectroscopy was used to evaluate the results of the exposure. Results: The results of this study showed that the Amide I vibration band increased in intensity with the increase of the frequency, leading us to assume that the displacement of the cell channels α-helices depends on the frequency of the applied electromagnetic fields. Conclusion: This preliminary result leads us to plan future research aimed at searching for the natural frequencies of membrane channels in tumor cells using resonant electromagnetic fields in order to damage the cellular functions of tumor cells. Clinical trials are needed to confirm such a hypothesis derived from this physical study.

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Section: Discussionsupporting

confidence: 86%

Section: Methodsmentioning

confidence: 99%

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New Perspectives in the Treatment of Tumor Cells by Electromagnetic Radiation at Resonance Frequencies in Cellular Membrane Channels

Calabrò¹,

Magazù²

2019

TOBIOTJ

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“…it has a quaternary structure with four identical subunits that are linked by non-covalent interactions such as hydrogen bonding and electrostatic interactions. This delicate equilibrium can be changed by exposure to HF-EMFs, such as it was shown in previous research [12,14,16,17].…”

Section: Introductionmentioning

confidence: 70%

Effects of the Addition of Sodium Chloride to a Tetrameric Protein in Water Solution During Exposure to High Frequency Electromagnetic Field

Calabrò¹,

Magazù²

2017

TOBIOTJ

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Background:Previous studies have shown that exposure to high frequency electromagnetic fields induces alterations in simple organic systems such as proteins in bidistilled water solution. Objective:The aim of this study was to test the shielding action of sodium chloride in bidistilled water solution against exposure to a high frequency electromagnetic field, in order to evaluate if the addition of NaCl in proteins aqueous solution can be considered a valuable bioprotector against electromagnetic fields. Method:Samples of 250 μl of different hemoglobin aqueous solutions, in the absence or presence of sodium-chloride, were exposed for 3 hours to an electromagnetic field at 1750 MHz at a power density around 1 W/m 2 emitted by an operational mobile phone. Fourier Transform Infrared Spectroscopy was used to study the effects of exposure on the secondary structure of hemoglobin also in the presence of sodium-chloride. Results:Spectral analysis evidenced that significant increase in intensity of the Amide I and II vibration bands in hemoglobin bidistilled water solution occurred after exposure to the electromagnetic field. This result can be due to the increase of dipole moment of the protein due to the alignment of α-helix towards the direction of the field. In contrast, no appreciable change was observed in hemoglobin in sodium-chloride water solution after exposure. Conclusion:This protective effect of sodium-chloride can be explained by the orientation of water molecules due to the strong electric field around each ion that reduces the possibility of rotation of the protein in response to an applied electromagnetic field.

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“…In particular, significant increase in intensity of β‐sheet content with respect to the α‐helix component was detected in the Amide I region of typical proteins in water solution after exposure to EMFs, showing that EMFs can induce unfolding process in the secondary structure of proteins [Calabrò and Magazù, , , , ; Magazù and Calabrò, ].…”

Section: Introductionmentioning

confidence: 99%

Induced‐orientation of nitrogen monoxide and azide ion vibrations in human hemoglobin in bidistilled water solution under a static magnetic field

Calabrò

Magazù

2017

Bioelectromagnetics

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In this study, we report the effects of static magnetic fields (SMFs) at 200 mT on different hemoglobin aqueous solutions, in the absence and in the presence of sucrose and trehalose, studied by FTIR spectroscopic techniques. Significant decrease in intensity of Amide I and Amide II vibration bands was observed after 6 h exposure for hemoglobin in bidistilled water solution. Also, it was observed that the decrease in intensity of the Amide I band was larger than the Amide II after exposure. This result can be explained assuming that an SMF induces increase of hydrogen bonding in hemoglobin in bidistilled water solution. In particular, the use of second-derivative analysis highlighted two absorption peaks at 1907 and 2022 cm that can be attributed to nitrogen monoxide vibration and antisymmetric stretch of azide ion bound, respectively. These vibrations increased significantly after exposure to the SMF (P < 0.01). This result can be explained assuming that exposure to an SMF induces the orientation of nitrogen monoxide and azide ion ligands toward the direction of the field. Finally, it was observed that the addition of sucrose and trehalose in hemoglobin aqueous solution inhibited such alterations, suggesting that bioprotective effectiveness of these disaccharides occurs after exposure to an SMF. Bioelectromagnetics. 38:447-455, 2017. © 2017 Wiley Periodicals, Inc.

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Parallel β‐sheet vibration band increases with proteins dipole moment under exposure to 1765 MHz microwaves

Cited by 22 publications

References 43 publications

New Perspectives in the Treatment of Tumor Cells by Electromagnetic Radiation at Resonance Frequencies in Cellular Membrane Channels

New Perspectives in the Treatment of Tumor Cells by Electromagnetic Radiation at Resonance Frequencies in Cellular Membrane Channels

Effects of the Addition of Sodium Chloride to a Tetrameric Protein in Water Solution During Exposure to High Frequency Electromagnetic Field

Induced‐orientation of nitrogen monoxide and azide ion vibrations in human hemoglobin in bidistilled water solution under a static magnetic field

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