ArticleScientific reports2017
Inert Gas Deactivates Protein Activity by Aggregation.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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12 citing papers in PubMed, 35 citations in OpenAlex.
- Aqueous photo-RAFT polymerization under ambient conditions: synthesis of protein-polymer hybrids in open air.Chemical science · 2024Article
- Studying the Effects of Dissolved Noble Gases and High Hydrostatic Pressure on the Spherical DOPC Bilayer Using Molecular Dynamic Simulations.Membranes · 2024Article
- Local Xenon-Protein Interaction Produces Global Conformational Change and Allosteric Inhibition in Lysozyme.Biochemistry · 2023Article
- Fully Oxygen-Tolerant Visible-Light-Induced ATRP of Acrylates in Water: Toward Synthesis of Protein-Polymer Hybrids.Macromolecules · 2023Article
- Programming xenon diffusion in maltose-binding protein.Biophysical journal · 2022Article
- Open-air green-light-driven ATRP enabled by dual photoredox/copper catalysis.Chemical science · 2022Article
- Fully oxygen-tolerant atom transfer radical polymerization triggered by sodium pyruvate.Chemical science · 2020Article
- Protein-polymer bioconjugates via a versatile oxygen tolerant photoinduced controlled radical polymerization approach.Nature communications · 2020Article
- The effect of high pressure on the NMDA receptor: molecular dynamics simulations.Scientific reports · 2019Article
- Surface-Templated Nanobubbles Protect Proteins from Surface-Mediated Denaturation.The journal of physical chemistry letters · 2019Article
- Xenon-Protein Interactions: Characterization by X-Ray Crystallography and Hyper-CEST NMR.Methods in enzymology · 2018Article
- Xenon as a transdermal enhancer for niacinamide in Strat-M™ membranes.Medical gas researchArticle
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Authors and funding
13 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Biologically inert gases play important roles in the biological functionality of proteins. However, researchers lack a full understanding of the effects of these gases since they are very chemically stable only weakly absorbed by biological tissues. By combining X-ray fluorescence, particle sizing and molecular dynamics (MD) simulations, this work shows that the aggregation of these inert gases near the hydrophobic active cavity of pepsin should lead to protein deactivation. Micro X-ray fluorescence spectra show that a pepsin solution can contain a high concentration of Xe or Kr after gassing, and that the gas concentrations decrease quickly with degassing time. Biological activity experiments indicate a reversible deactivation of the protein during this gassing and degassing. Meanwhile, the nanoparticle size measurements reveal a higher number of "nanoparticles" in gas-containing pepsin solution, also supporting the possible interaction between inert gases and the protein. Further, MD simulations indicate that gas molecules can aggregate into a tiny bubble shape near the hydrophobic active cavity of pepsin, suggesting a mechanism for reducing their biological function.
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