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Aggregated gas molecules: toxic to protein?
Meng Zhang1, Guanghong Zuo, Jixiu Chen
1Division of Interfacial Water and Laboratory of Physical Biology, Shanghai Institute of Applied Physics, Chinese Academy of Sciences, PO Box 800-204, Shanghai 201800, China.
Scientific Reports
|April 17, 2013
Summary
High levels of breathing gases can be toxic. Aggregated nitrogen molecules bind to protein active sites, potentially impairing protein function, unlike dispersed molecules.
Area of Science:
- Biochemistry
- Physical Chemistry
- Molecular Biology
Background:
- Biological toxicity of high gas concentrations is known but poorly understood.
- Previous research focused on dissolved gas molecules' effects on biomolecules.
- Recent findings indicate aggregated gas molecules exist at water-solid interfaces.
Purpose of the Study:
- Investigate the binding preference of aggregated gas molecules on proteins.
- Utilize molecular dynamics simulations for this investigation.
- Employ nitrogen (N₂) gas and the Src-homology 3 (SH3) domain as a model system.
Main Methods:
- Molecular dynamics simulations.
- Modeling aggregated nitrogen (N₂) molecules.
- Using the Src-homology 3 (SH3) domain as a model protein.
Main Results:
- Aggregated N₂ molecules showed strong binding to the SH3 domain's active sites.
- This binding has the potential to impair protein activity.
- Dispersed N₂ molecules did not exhibit specific interactions with the SH3 domain.
Conclusions:
- Aggregated gas molecules, not dispersed ones, interact specifically with protein active sites.
- This specific binding mechanism offers insight into gas molecule toxicity.
- Findings advance the understanding of gas aggregate toxicity in protein function.
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