Inert gas deactivates protein activity by aggregation

Zhang, L, Zhang, Y, Cheng, J, Wang, L, Wang, X, Zhang, M, Gao, Y, Hu, J, Zhang, X, Lu, J, Li, G, Tai, R and Fang, H 2017, 'Inert gas deactivates protein activity by aggregation', Scientific Reports, vol. 7, no. 1, pp. 1-8.


Document type: Journal Article
Collection: Journal Articles

Title Inert gas deactivates protein activity by aggregation
Author(s) Zhang, L
Zhang, Y
Cheng, J
Wang, L
Wang, X
Zhang, M
Gao, Y
Hu, J
Zhang, X
Lu, J
Li, G
Tai, R
Fang, H
Year 2017
Journal name Scientific Reports
Volume number 7
Issue number 1
Start page 1
End page 8
Total pages 8
Publisher Nature
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.
Subject Physical Chemistry not elsewhere classified
Chemical Sciences not elsewhere classified
Keyword(s) Der-Waals Complexes
Xenon
Binding
XE
Myoglobin
Pathways
Nitrogen
Cavity
KR
Ionization
DOI - identifier 10.1038/s41598-017-10678-3
Copyright notice © 2017 The Author(s). Open Access This article is licensed under a Creative Commons Attribution 4.0
ISSN 2045-2322
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