Structural Analysis of Plasma-Induced Oxidation and Electric Field Effect on the Heat Shock Protein (Hsp60) Structure

Overview

There is a growing interest in understanding the mechanisms behind plasma oncology, leading to extensive wet lab and computational research. Computational approaches are particularly advantageous for analyzing protein structures impacted by plasma treatment, given the difficulty in obtaining sufficient protein quantities for traditional biophysical analysis.

Study Focus

• Investigation of plasma-induced oxidation and electric field effects on the human mitochondrial heat shock protein (mHsp60), a highly conserved chaperonin crucial across species.
• Molecular dynamics simulations were used to calculate root-mean-square deviation (RMSD), root-mean-square fluctuation (RMSF), and solvent-accessible surface area of mHsp60 in both oxidized and non-oxidized states.
• Different electric field strengths were applied (0.003 and 2.0 V/nm) to examine their impact on mHsp60 structure.

Findings

• Electric fields exerted a stronger disruptive effect on the structure of mHsp60 than oxidation alone.
• The combination of oxidation and electric field led to significantly increased destabilization of the Hsp60 structure compared to either treatment alone or controls.
• Plasma-assisted oxidation targeting specific amino acids (Trp, Tyr, and Met) altered mHsp60 structure, with oxidation of Met increasing flexibility and other oxidation events causing rigidity.
• Electric field applications increased RMSD values especially in native mHsp60 compared to oxidized forms, suggesting a heightened susceptibility of the non-oxidized protein.
• Notably, even small electric fields generated by DBD plasma caused substantive conformational changes in both native and oxidized protein.

Conclusion

Hsp60 and other heat shock proteins are critical for protein homeostasis, cellular integrity, survival, and metabolism. The study demonstrates that exposure to electric fields—such as those found in various electromagnetic field environments—and oxidation can compromise chaperone-assisted protein quality control. Such disruption is connected to the triggering and progression of numerous diseases, underlining the vital link between electromagnetic field exposure and potential health risks.