Electromagnetic field modulates aggregation propensity of amyloid peptides

Authors: Todorova N, Bentvelzen A, Yarovsky I

Year: 2020 Jan 21

Category: Biophysics

Journal: J Chem Phys

DOI: 10.1063/1.5126367

URL: https://aip.scitation.org/doi/10.1063/1.5126367

Abstract

Overview

The impact of nonthermal electromagnetic (EM) fields on biological molecules, particularly in the radio and microwave frequency ranges, is poorly understood due to challenges in detection.

Methodology

This study utilized all-atom nonequilibrium molecular dynamics simulations to explore the response of amyloidogenic peptides to nonionizing EM radiation under various field characteristics.

Findings

  • The study demonstrated that the EM field influences peptide conformations which are both frequency and strength dependent.
  • High field strength (0.7 V/nmrms) led to wider conformational exploration by the peptides.
  • At medium field strengths (0.07-0.0385 V/nmrms) and lower frequencies, peptides showed fibril-forming and inhibitory conformations.
  • The highest frequency (5.0 GHz) induced increased peptide dynamics and extended conformations, promoting structures supportive of fibril formation.

Conclusion

The interaction between peptides and specific EM field parameters can either inhibit or promote the formation of amyloid fibrils. Such insights are critical, suggesting that controlled application of EM fields might play a role in managing amyloid diseases or in material engineering.

electromagnetic fields amyloid peptides molecular dynamics simulations nonionizing radiation protein aggregation
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