Interaction of human arylamine n-acetyltransferase 1 with different nanomaterials

Deng, Zhou J., Butcher, Neville J., Mortimer, Gysell M., Jia, Zhongfan, Monteiro, Michael J., Martin, Darren J. and Minchin, Rodney F. (2014) Interaction of human arylamine n-acetyltransferase 1 with different nanomaterials. Drug Metabolism and Disposition, 42 3: 377-383. doi:10.1124/dmd.113.055988

Author Deng, Zhou J.
Butcher, Neville J.
Mortimer, Gysell M.
Jia, Zhongfan
Monteiro, Michael J.
Martin, Darren J.
Minchin, Rodney F.
Title Interaction of human arylamine n-acetyltransferase 1 with different nanomaterials
Journal name Drug Metabolism and Disposition   Check publisher's open access policy
ISSN 0090-9556
Publication date 2014
Year available 2013
Sub-type Article (original research)
DOI 10.1124/dmd.113.055988
Open Access Status
Volume 42
Issue 3
Start page 377
End page 383
Total pages 7
Place of publication Bethesda, MD United States
Publisher American Society for Pharmacology and Experimental Therapeutics
Collection year 2014
Language eng
Subject 3004 Pharmacology
3003 Pharmaceutical Science
Abstract Humans are exposed to nanoparticles in the environment as well as those in nanomaterials developed for biomedical applications. However, the safety and biologic effects of many nanoparticles remain to be elucidated. Over the past decade, our understanding of the interaction of proteins with various nanomaterials has grown. The protein corona can determine not only how nanoparticles interact with cells but also their biologic effects and toxicity. In this study, we describe the effects that several different classes of nanoparticles exert on the enzymatic activity of the cytosolic protein human arylamine N-acetyltransferase 1 (NAT1), a drug-metabolizing enzyme widely distributed in the body that is also responsible for the activation and detoxification of known carcinogens. We investigated three metal oxides (zinc oxide, titanium dioxide, and silicon dioxide), two synthetic clay nanoparticles (layered double hydroxide and layered silicate nanoparticles), and a self-assembling thermoresponsive polymeric nanoparticle that differ in size and surface characteristics. We found that the different nanoparticles induced very different responses, ranging from inhibition to marked enhancement of enzyme activity. The layered silicates did not directly inactivate NAT1, but was found to enhance substrate-dependent inhibition. These differing effects demonstrate the multiplicity of nanoparticle-protein interactions and suggest that enzyme activity may be compromised in organs exposed to nanoparticles, such as the lungs or reticulo-endothelial system. Copyright
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

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