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The cellular response and molecular mechanism of superoxide dismutase interacting with superparamagnetic iron oxide nanoparticles.
Ju, Hao; Liu, Yue; Wang, Yameng; Lu, Rui; Yang, Bin; Wang, Deyi; Wang, Jing.
Afiliación
  • Ju H; School of Environmental and Material Engineering, Yantai University, 30# Qingquan Road, Yantai 264005, PR China.
  • Liu Y; College of Life Science, Institute of Life Science and Green Development, Hebei University, Baoding 071002, PR China.
  • Wang Y; Chinese Academy for Environmental Planning, Building 1, No. 15, Shixing Street, Shijingshan District, Beijing 100041, PR China.
  • Lu R; Test Experiment Center, Shandong Institute of Space Electronic Technology, 513# Hangtian Road, Yantai 264670, PR China.
  • Yang B; School of Environmental and Material Engineering, Yantai University, 30# Qingquan Road, Yantai 264005, PR China.
  • Wang D; School of Environmental and Material Engineering, Yantai University, 30# Qingquan Road, Yantai 264005, PR China. Electronic address: wangdy107@163.com.
  • Wang J; School of Environmental and Material Engineering, Yantai University, 30# Qingquan Road, Yantai 264005, PR China. Electronic address: ufowjing@ytu.edu.cn.
NanoImpact ; 35: 100515, 2024 Jul.
Article en En | MEDLINE | ID: mdl-38857755
ABSTRACT
This study explored the response of superoxide dismutase (SOD) under superparamagnetic iron oxide nanoparticles (SPIONs)-induced oxidative stress using combined cellular and molecular methods. Results found that SPIONs induced the inhibition of catalase activity, the U-inverted change of SOD activity and the accumulation of reactive oxygen species (ROS), leading to oxidative damage and cytotoxicity. The change of intracellular SOD activity was resulted from the increase of molecular activity induced by directly interacting with SPIONs and ROS-inhibition of activity. The increase of molecular activity could be attributed to the structural and conformational changes of SOD, which were caused by the direct interaction of SOD with SPIONs. The SOD-SPIONs interaction and its interacting mechanism were explored by multi-spectroscopy, isothermal titration calorimetry and zeta potential assays. SOD binds to SPIONs majorly via hydrophobic forces with the involvement of electrostatic forces. SPIONs approximately adsorb 11 units of SOD molecule with the binding affinity of 2.99 × 106 M-1. The binding sites on SOD were located around Tyr residues, whose hydrophilicity increased upon interacting with SPIONs. The binding to SPIONs loosened the peptide chains, changed the secondary structure and reduced the aggregation state of SOD.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Superóxido Dismutasa / Especies Reactivas de Oxígeno / Nanopartículas Magnéticas de Óxido de Hierro Límite: Animals / Humans Idioma: En Revista: NanoImpact Año: 2024 Tipo del documento: Article Pais de publicación: Países Bajos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Superóxido Dismutasa / Especies Reactivas de Oxígeno / Nanopartículas Magnéticas de Óxido de Hierro Límite: Animals / Humans Idioma: En Revista: NanoImpact Año: 2024 Tipo del documento: Article Pais de publicación: Países Bajos