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Area of Science:

  • Biochemistry
  • Biophysics
  • Computational Biology

Background:

  • Biologically inert gases are chemically stable and weakly absorbed by tissues.
  • Understanding their effects on protein functionality is limited.
  • Pepsin's biological activity is crucial in various biological processes.

Purpose of the Study:

  • To investigate the impact of inert gases (Xe, Kr) on pepsin's biological activity.
  • To elucidate the mechanism of protein deactivation by inert gases.
  • To explore the interaction between inert gases and protein structures.

Main Methods:

  • Micro X-ray fluorescence spectroscopy to quantify gas concentrations.
  • Particle sizing to detect nanoparticle formation.
  • Molecular dynamics (MD) simulations to model gas-protein interactions.
  • Biological activity assays to measure protein function.

Main Results:

  • Pepsin solutions showed high concentrations of Xe and Kr after gassing, which decreased upon degassing.
  • Protein deactivation was observed during gassing and reversed upon degassing.
  • Increased nanoparticle formation in gas-containing solutions suggested gas-protein interaction.
  • MD simulations revealed gas molecule aggregation near pepsin's hydrophobic active cavity.

Conclusions:

  • Inert gas aggregation near pepsin's active cavity leads to reversible protein deactivation.
  • This aggregation mechanism explains the observed reduction in biological function.
  • The study provides insights into inert gas interactions with proteins.