Effects of oscillating electric fields on conotoxin peptide conformation: A molecular dynamic simulation study

Jain, Shubhendra Kumar; Suresh, Abishek; Pirogova, Elena

doi:10.1016/j.jmgm.2020.107799

Cited by 9 publications

(6 citation statements)

References 31 publications

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“…Dean et al simulated the M-1 conotoxin protein under the oscillating electric fields of strengths 2, 6, and 47 V/m at the frequency of 1800 MHz. 14 The results showed that the conformation of the toxin changed at 47 V/m electric field, but changed very little at 6 V/m electric field, and the lowest electric field of 2 V/m had no effect on the conformation of the toxin. Cifra and Prusǎ analyzed the influence of the parameters of molecular force field on dielectric spectrum.…”

Section: Introductionmentioning

confidence: 93%

“…The molecular mechanism of the nonthermal effect of microwaves has been studied deeply. − Yarovsky et al used molecular dynamics simulation to study the structure, side-chain orientation, aggregation tendency, and dipole moment orientation of polypeptides in a microwave field . The results showed that different intensities and frequencies of the microwave field induced specific polypeptide structure.…”

Section: Introductionmentioning

confidence: 99%

“…The conformations of proteins are changed by the thermal stress and electric field. Dean et al simulated the M-1 conotoxin protein under the oscillating electric fields of strengths 2, 6, and 47 V/m at the frequency of 1800 MHz . The results showed that the conformation of the toxin changed at 47 V/m electric field, but changed very little at 6 V/m electric field, and the lowest electric field of 2 V/m had no effect on the conformation of the toxin.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Molecular Dynamics Research of Spatial Orientation and Kinetic Energy of Active Site Collision of Carnosine under Weak Microwave Irradiation

et al. 2022

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The molecular mechanism of the microwave nonthermal effect is still not clear. This work investigated the spatial orientation and kinetic energy of active site collision of carnosine, a natural bioactive dipeptide, under the weak microwave irradiation using the molecular dynamics simulation. Our results showed the influences of the temperature, microwave intensity, microwave frequency, and microwave polarization mode (linear polarization and circular polarization) on the spatial orientation and kinetic energy of active site collision of carnosine. First, under the constant intensity and frequency of linear polarization microwave irradiation, the increment of the collision probability between the 6N atom of carnosine and the 28H atom of the other carnosine at effective space angle decreases from 85.0% to 3.5% with increasing temperature. Second, with the increase of microwave intensity, the change of spatial orientation and kinetic energy becomes more and more significant. However, the change of circular polarization microwaves on the spatial orientation and kinetic energy of collision is weaker than that of linear polarization. Third, under the constant intensity of linear polarization microwave irradiation, the collision probability between the 6N atom and the 28H atom at effective space angle decreases from 70.2% to 14.7% with increasing frequency. Finally, under the microwave polarization, the spatial orientation and kinetic energy of molecular collision are changed, which is summarized as the microwave postpolarization effect (MWPPE). The dependence of MWPPE on temperature, microwave intensity, microwave frequency, and polarization mode is very complicated. In the end, this effect can provide a new insight into the molecular mechanism of the microwave nonthermal effect.

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Section: Introductionmentioning

confidence: 93%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Molecular Dynamics Research of Spatial Orientation and Kinetic Energy of Active Site Collision of Carnosine under Weak Microwave Irradiation

et al. 2022

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“…By stimulating proteases according to this property to change their secondary structure and, thus, affect the function or properties of proteases, the catalytic process can be precisely controlled to achieve the goals of clinical precision treatment and maximizing production benefits. Many factors affect the structure of proteins, and a large number of studies have shown that exogenous factors such as pressure [8], temperature [9][10][11], ion concentration [11], irradiation [12], PH [13], the electric field [14][15][16], and magnetic field [17] affect protein conformation stability.…”

Section: Introductionmentioning

confidence: 99%

Molecular Study on Conformational Changes in Trypsin Inhibitors in Multidirectional Electrostatic Fields

Hou,

Zheng,

Chu

et al. 2024

Applied Sciences

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Proteins undergo a series of conformational changes when affected by the applied electric field, which changes their functions and properties. The conformational changes in proteins in various electric fields are different due to their internal structures. This study simulates the molecular dynamics of proteins in different amounts and directions of electric fields with gromacs software. According to the root mean square deviation, hydrogen bond, dipole moment, and solvent accessible surface area, it is proved that the conformation change in proteins is more drastic under the simultaneous action of multiple electric fields under various directions, and different fragments unfold with divergent electric fields combined, which is of great importance to control protein function, improve biochemical research and production efficiency in the food and drug safety field.

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“…Recently, the focus of neurodegenerative disease research has been shifted towards the molecular level: on the effects of electric field on protein conformation, aggregation, and fibril formation. It has already been shown that different electric field modalities, such as oscillating [ 30 , 31 ] and static fields [ 32 , 33 ] can induce significant structural changes in amylogenic proteins [ 34 , 35 ] and disrupt aggregations and fibrils [ 36 ]. Studies also report electric field-induced changes in activity [ 37 , 38 ], hydration [ 39 ], and adsorption [ 40 ] of proteins.…”

Section: Introductionmentioning

confidence: 99%

Effect of Electric Field on α-Synuclein Fibrils: Revealed by Molecular Dynamics Simulations

Razzokov

Fazliev

Makhkamov³

et al. 2023

IJMS

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The self-association of amylogenic proteins to the fibril form is considered a pivotal factor in the pathogenesis of neurodegenerative diseases, including Parkinson’s disease (PD). PD causes unintended or uncontrollable movements in its common symptoms. α-synuclein is the major cause of PD development and thus has been the main target of numerous studies to suppress and sequester its expression or effectively degrade it. Nonetheless, to date, there are no efficient and proven ways to prevent pathological protein aggregation. Recent investigations proposed applying an external electric field to interrupt the fibrils. This method is a non-invasive approach that has a certain benefit over others. We performed molecular dynamics (MD) simulations by applying an electric field on highly toxic fibrils of α-synuclein to gain a molecular-level insight into fibril disruption mechanisms. The results revealed that the applied external electric field induces substantial changes in the conformation of the α-synuclein fibrils. Furthermore, we show the threshold value for electric field strength required to completely disrupt the α-synuclein fibrils by opening the hydrophobic core of the fibril. Thus, our findings might serve as a valuable foundation to better understand molecular-level mechanisms of the α-synuclein fibrils disaggregation process under an applied external electric field.

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Effects of oscillating electric fields on conotoxin peptide conformation: A molecular dynamic simulation study

Cited by 9 publications

References 31 publications

Molecular Dynamics Research of Spatial Orientation and Kinetic Energy of Active Site Collision of Carnosine under Weak Microwave Irradiation

Molecular Dynamics Research of Spatial Orientation and Kinetic Energy of Active Site Collision of Carnosine under Weak Microwave Irradiation

Molecular Study on Conformational Changes in Trypsin Inhibitors in Multidirectional Electrostatic Fields

Effect of Electric Field on α-Synuclein Fibrils: Revealed by Molecular Dynamics Simulations

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