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Aggregated gas molecules: toxic to protein?


ABSTRACT: The biological toxicity of high levels of breathing gases has been known for centuries, but the mechanism remains elusive. Earlier work mainly focused on the influences of dispersed gas molecules dissolved in water on biomolecules. However, recent studies confirmed the existence of aggregated gas molecules at the water-solid interface. In this paper, we have investigated the binding preference of aggregated gas molecules on proteins with molecular dynamics simulations, using nitrogen (N?) gas and the Src-homology 3 (SH3) domain as the model system. Aggregated N? molecules were strongly bound by the active sites of the SH3 domain, which could impair the activity of the protein. In contrast, dispersed N? molecules did not specifically interact with the SH3 domain. These observations extend our understanding of the possible toxicity of aggregates of gas molecules in the function of proteins.

SUBMITTER: Zhang M 

PROVIDER: S-EPMC3627187 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature

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Aggregated gas molecules: toxic to protein?

Zhang Meng M   Zuo Guanghong G   Chen Jixiu J   Gao Yi Y   Fang Haiping H  

Scientific reports 20130101


The biological toxicity of high levels of breathing gases has been known for centuries, but the mechanism remains elusive. Earlier work mainly focused on the influences of dispersed gas molecules dissolved in water on biomolecules. However, recent studies confirmed the existence of aggregated gas molecules at the water-solid interface. In this paper, we have investigated the binding preference of aggregated gas molecules on proteins with molecular dynamics simulations, using nitrogen (N₂) gas an  ...[more]

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