Surface Coating Rescues Proteins from Magnetite Nanoparticle Induced Damage

Authors

  • Nidhi Joshi,

    1. Protein Folding and Dynamics Laboratory Structural Biology and Bioinformatics Division, CSIR-Indian Institute of Chemical Biology, Kolkata, India
    Search for more papers by this author
  • Anindita Mukhopadhyay,

    1. Nano-Structured Materials Division, CSIR-Central Glass and Ceramics Research Institute, Kolkata, India
    Search for more papers by this author
  • Sujit Basak,

    1. Protein Folding and Dynamics Laboratory Structural Biology and Bioinformatics Division, CSIR-Indian Institute of Chemical Biology, Kolkata, India
    Search for more papers by this author
  • Goutam De,

    Corresponding author
    1. Nano-Structured Materials Division, CSIR-Central Glass and Ceramics Research Institute, Kolkata, India
    • Protein Folding and Dynamics Laboratory Structural Biology and Bioinformatics Division, CSIR-Indian Institute of Chemical Biology, Kolkata, India
    Search for more papers by this author
  • Krishnananda Chattopadhyay

    Corresponding author
    • Protein Folding and Dynamics Laboratory Structural Biology and Bioinformatics Division, CSIR-Indian Institute of Chemical Biology, Kolkata, India
    Search for more papers by this author

E-mail: gde@cgcri.res.in, krish@iicb.res.in

Abstract

The presence of magnetic nanoparticles (NPs) in physiological systems induces toxicity through its effects on mitochondrial function and reactive oxygen species (ROS) imbalance. Magnetic NP induced cytotoxicity has been elaborately evaluated for impending threats, however, a detailed investigation is lacking. It is shown that the interaction of Fe3O4 NPs with cytochrome c can lead to different events based on the NPs to protein ratio, the solution conditions, and the type of surface protection. At low NPs concentration, rapid binding and subsequent electron transfer are the preferred events while at higher concentration slow oxidative modification of the protein is initiated. The slow event of protein modification yields conformational disorientation, loss of stability, and formation of amyloid-like structures with cytochrome c. The possibility that the NP induced oxidative stress and age can work in concert to compromise different aspects of cellular quality control processes is discussed. Suitable surface modifications of the NPs inhibit their direct binding to the protein molecules and minimize NP induced toxicity.

Ancillary