Structural Analysis of Plasma-Induced Oxidation and Electric Field Effect on the Heat Shock Protein
Abstract
Structural Analysis of Plasma-Induced Oxidation and Electric Field Effect on the Heat Shock Protein (Hsp60) Structure Attri P, Okumura T, Koga K, Shiratani M. Structural Analysis of Plasma-Induced Oxidation and Electric Field Effect on the Heat Shock Protein (Hsp60) Structure: A Computational Viewpoint. Chem Biodivers. 2025 Jan 5:e202401243. doi: 10.1002/cbdv.202401243. Abstract In recent years, there has been an increase in the study of the mechanisms behind plasma oncology. For this, many wet lab experiments and computational studies were conducted. Computational studies give an advantage in examining protein structures that are costly to extract in enough amounts to analyze the biophysical properties following plasma treatment. Therefore, in this work, we studied the effect of plasma oxidation and electric field on the human mitochondrial heat shock protein (mHsp60). Hsp60, alias chaperonin, is one of the most conserved proteins expressed across all species. Hence, we performed molecular dynamic simulations to calculate the root-mean-square deviation, root-mean- square fluctuation, and solvent-accessible surface area of mHsp60 with and without oxidation. In addition to the oxidation state, we also applied an electric field (0.003 and 2.0 V/nm) to check the changes in the mHsp60 protein. Through simulations, we observed that the electric field strongly affects the structure of mHsp60 protein compared with the oxidation. The combination of oxidation and electric field effect increases the destabilization of the mHsp60 structure compared with their respective control states. pubmed.ncbi.nlm.nih.gov Conclusion We can conclude that the mHsp60 structure is modified by possible plasma-assisted oxidation, particularly involving Trp, Try, and Met amino acids, resulting in noticeable structural changes. RMSD values reflect that mHsp60 structure flexibility slightly increases in OXID-2, whereas the structure becomes rigid in OXID-1. This suggests that the oxidation of Met amino acids plays a significant role in enhancing mHsp60 flexibility. On the other hand, applying an electric field (EF1 and EF2) to the control mHsp60 increases the RMSD value more than for oxidized mHsp60 (OXID-1 and OXID-2), indicating that the electric field has a more substantial effect on the mHsp60 structure than oxida- tion alone. Additionally, the RMSD values of OXID-1 and OXID-2 increased after electric field treatment (0.003 V/nm from the x, y, and z axes), demonstrating that the small electric field generated by DBD plasma can significantly influence protein conforma- tional changes in both native and oxidized states. HSPs, including Hsp60, play a vital role in maintaining protein homeostasis, which is crucial for cell integrity, survival, and metabolism. However, when chaperone-assisted protein quality control is compromised due to oxidation or exposure to electric effect, it may trigger the onset and progression of numerous diseases.
AI evidence extraction
Main findings
Using molecular dynamics simulations of human mitochondrial Hsp60 (mHsp60), the authors report that applying an electric field (0.003 and 2.0 V/nm) affected mHsp60 structure more strongly than plasma-induced oxidation alone. They report that combining oxidation with electric field exposure increased destabilization relative to respective control states.
Outcomes measured
- Protein structural stability/conformational change (mHsp60)
- Root-mean-square deviation (RMSD)
- Root-mean-square fluctuation (RMSF)
- Solvent-accessible surface area (SASA)
Limitations
- Computational (molecular dynamics) study rather than biological/clinical outcomes
- Exposure context is modeled (electric field values applied in simulation) and may not directly translate to real-world EMF exposures
- No sample size or replication details provided in the abstract
View raw extracted JSON
{
"publication_year": null,
"study_type": "in_vitro",
"exposure": {
"band": null,
"source": "plasma-associated electric field (DBD plasma context)",
"frequency_mhz": null,
"sar_wkg": null,
"duration": null
},
"population": null,
"sample_size": null,
"outcomes": [
"Protein structural stability/conformational change (mHsp60)",
"Root-mean-square deviation (RMSD)",
"Root-mean-square fluctuation (RMSF)",
"Solvent-accessible surface area (SASA)"
],
"main_findings": "Using molecular dynamics simulations of human mitochondrial Hsp60 (mHsp60), the authors report that applying an electric field (0.003 and 2.0 V/nm) affected mHsp60 structure more strongly than plasma-induced oxidation alone. They report that combining oxidation with electric field exposure increased destabilization relative to respective control states.",
"effect_direction": "harm",
"limitations": [
"Computational (molecular dynamics) study rather than biological/clinical outcomes",
"Exposure context is modeled (electric field values applied in simulation) and may not directly translate to real-world EMF exposures",
"No sample size or replication details provided in the abstract"
],
"evidence_strength": "low",
"confidence": 0.7399999999999999911182158029987476766109466552734375,
"peer_reviewed_likely": "unknown",
"stance": "concern",
"stance_confidence": 0.6999999999999999555910790149937383830547332763671875,
"summary": "This computational study used molecular dynamics simulations to examine how plasma-associated oxidation and applied electric fields (0.003 and 2.0 V/nm) influence the structure of human mitochondrial Hsp60 (mHsp60). The authors report that electric field exposure produced larger structural effects than oxidation alone, and that combining oxidation with electric field increased destabilization compared with controls. The paper frames these structural changes as potentially relevant to compromised chaperone function.",
"key_points": [
"The study models plasma-induced oxidation effects on mHsp60 and compares them with applied electric field effects.",
"Simulations assessed RMSD, RMSF, and solvent-accessible surface area to characterize structural changes.",
"Electric fields (0.003 and 2.0 V/nm) were reported to alter mHsp60 structure more than oxidation alone.",
"Oxidation was described as involving Trp, Tyr, and Met residues, with Met oxidation suggested to influence flexibility.",
"Applying a small electric field (0.003 V/nm) was reported to increase RMSD in both native and oxidized states.",
"The authors suggest that oxidation or electric-field-related effects on chaperones could compromise protein quality control, with potential disease relevance."
],
"categories": [
"Mechanisms",
"In Vitro & Molecular",
"Protein & Oxidative Stress"
],
"tags": [
"Molecular Dynamics",
"Electric Field Exposure",
"Plasma Medicine",
"DBD Plasma",
"Protein Conformation",
"Heat Shock Protein 60",
"Chaperone Proteins",
"Protein Oxidation",
"Mitochondrial Proteins",
"RMSD",
"RMSF",
"Solvent Accessible Surface Area"
],
"keywords": [
"Hsp60",
"mHsp60",
"plasma oxidation",
"electric field",
"molecular dynamic simulations",
"RMSD",
"RMSF",
"SASA",
"DBD plasma",
"protein destabilization"
],
"suggested_hubs": [],
"social": {
"tweet": "MD simulations of human mitochondrial Hsp60 report that applied electric fields (0.003–2.0 V/nm) altered protein structure more than plasma-induced oxidation, with combined oxidation+field increasing destabilization vs controls.",
"facebook": "A computational (molecular dynamics) study of human mitochondrial Hsp60 reports that applied electric fields (0.003 and 2.0 V/nm) produced stronger structural changes than plasma-induced oxidation alone, and that combining oxidation with electric field increased destabilization compared with controls.",
"linkedin": "This molecular dynamics study modeled plasma-induced oxidation and applied electric fields (0.003 and 2.0 V/nm) on human mitochondrial Hsp60, reporting larger structural effects from electric fields than oxidation alone and greater destabilization when combined."
}
}
AI can be wrong. Always verify against the paper.
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