Electromagnetic field modulates aggregation propensity of amyloid peptides

2020 · Mixed · Very low evidence

← Research stream

MixedVery low evidencePaper 1613

Study snapshot

Publicationmanual · 2020

Study typein_vitro

Reported directionMixed

Evidence ratingVery low

Abstract

Electromagnetic field modulates aggregation propensity of amyloid peptides Todorova N, Bentvelzen A, Yarovsky I. Electromagnetic field modulates aggregation propensity of amyloid peptides. J Chem Phys. 2020 Jan 21;152(3):035104. doi: 10.1063/1.5126367. Abstract Nonthermal effects of the electromagnetic (EM) field in the radio and microwave frequency ranges on basic biological matter are difficult to detect and thus remain poorly understood. In this work, all-atom nonequilibrium molecular dynamics simulations were performed to investigate the molecular mechanisms of an amyloidogenic peptide response to nonionizing radiation of varying field characteristics. The results showed that the EM field induced peptide conformations dependent on the field frequency and strength. At the high field strength (0.7 V/nmrms), the peptide explored a wider conformational space as the frequency increased from 1.0 to 5.0 GHz. At the intermediate strength fields (0.07-0.0385 V/nmrms), the frequencies of 1.0 and 2.5 GHz resulted in the peptide being trapped in specific conformations, with 1.0 GHz enabling both fibril-forming and fibril-inhibiting conformations, while 2.5 GHz led to formation of mostly fibril-forming conformations. In contrast, the 5.0 GHz frequency caused increased peptide dynamics and more extended conformations with fibril-enabling aromatic side-chain arrangement akin to the structures formed under ambient conditions. All the simulated frequencies at low strength fields (0.007-0.0007 V/nmrms) resulted in the formation of amyloid-prone hairpin conformations similar to those formed under the weak static electric field and ambient conditions. These results suggest that specific ranges of EM field parameters produce peptide conformations unfavorable for formation of amyloid fibrils, a phenomenon that can be exploited in treatment and prevention of amyloid diseases. Alternatively, EM field parameters can be selected to modulate the formation of well-ordered peptide assemblies as a rational design strategy for engineering biocompatible materials. Open access paper: aip.scitation.org

Machine Enhanced Logic

AI evidence extraction

Structured fields below were generated from the paper’s abstract and metadata to make the evidence easier to inspect. Automated extraction may be incomplete or incorrect; verify important details against the original paper.

Study typein_vitro

Effect directionmixed

PopulationNot supplied

Sample sizeNot supplied

ExposureRF

Evidence strengthVery lowConfidence: 74% · Peer reviewed: yes

Main findings

All-atom nonequilibrium molecular dynamics simulations indicated that applied EM fields in the 1.0–5.0 GHz range induced peptide conformations that depended on field frequency and strength. Intermediate-strength fields produced frequency-dependent trapping in specific conformations (1.0 GHz enabling both fibril-forming and fibril-inhibiting conformations; 2.5 GHz mostly fibril-forming), while 5.0 GHz increased dynamics and more extended conformations; low-strength fields yielded amyloid-prone hairpin conformations similar to weak static electric field and ambient conditions.

Outcomes measured

Amyloidogenic peptide conformations
Aggregation/amyloid fibril-forming propensity (conformational indicators)
Peptide dynamics and conformational space explored

Limitations

Simulation study (all-atom nonequilibrium molecular dynamics), not an experimental biological/clinical study
Nonthermal effects inferred from modeled peptide conformations; no direct health outcomes assessed in the abstract
Exposure metrics reported as electric field strength (V/nmrms); SAR not provided

View raw extracted JSON

{
  "study_type": "in_vitro",
  "exposure": {
    "band": "RF",
    "source": null,
    "frequency_mhz": null,
    "sar_wkg": null,
    "duration": null
  },
  "population": null,
  "sample_size": null,
  "outcomes": [
    "Amyloidogenic peptide conformations",
    "Aggregation/amyloid fibril-forming propensity (conformational indicators)",
    "Peptide dynamics and conformational space explored"
  ],
  "main_findings": "All-atom nonequilibrium molecular dynamics simulations indicated that applied EM fields in the 1.0–5.0 GHz range induced peptide conformations that depended on field frequency and strength. Intermediate-strength fields produced frequency-dependent trapping in specific conformations (1.0 GHz enabling both fibril-forming and fibril-inhibiting conformations; 2.5 GHz mostly fibril-forming), while 5.0 GHz increased dynamics and more extended conformations; low-strength fields yielded amyloid-prone hairpin conformations similar to weak static electric field and ambient conditions.",
  "effect_direction": "mixed",
  "limitations": [
    "Simulation study (all-atom nonequilibrium molecular dynamics), not an experimental biological/clinical study",
    "Nonthermal effects inferred from modeled peptide conformations; no direct health outcomes assessed in the abstract",
    "Exposure metrics reported as electric field strength (V/nmrms); SAR not provided"
  ],
  "evidence_strength": "very_low",
  "confidence": 0.74,
  "peer_reviewed_likely": "yes",
  "keywords": [
    "radiofrequency",
    "microwave",
    "nonthermal effects",
    "molecular dynamics",
    "amyloidogenic peptide",
    "amyloid fibrils",
    "aggregation",
    "GHz",
    "electric field strength"
  ],
  "suggested_hubs": []
}

AI can be wrong. Always verify against the paper.

AI-extracted fields are generated from the abstract and metadata and may be incomplete or incorrect. This material is for informational purposes and is not medical advice.

Identifiers and source

DOI: 10.1063/1.5126367
PubMed: Not supplied

Read the original paper →

Related papers

← Back to the Research Library