Enzyme-Mimic Activity of Ferric Nano-Core Residing in Ferritin and Its Biosensing Applications
journal contributionposted on 22.02.2016 by Zhiwen Tang, Hong Wu, Youyu Zhang, Zhaohui Li, Yuehe Lin
Any type of content formally published in an academic journal, usually following a peer-review process.
Ferritins are nanoscale globular protein cages encapsulating a ferric core. They widely exist in animals, plants, and microbes, playing indispensable roles in iron homeostasis. Interestingly, our study clearly demonstrates that ferritin has an enzyme-mimic activity derived from its ferric nanocore but not the protein cage. Further study revealed that the mimic-enzyme activity of ferritin is more thermally stable and pH-tolerant compared with horseradish peroxidase. Considering the abundance of ferritin in numerous organisms, this finding may indicate a new role of ferritin in antioxidant and detoxification metabolisms. In addition, as a natural protein-caged nanoparticle with an enzyme-mimic activity, ferritin is readily conjugated with biomolecules to construct nanobiosensors, thus holds promising potential for facile and biocompatible labeling for sensitive and robust bioassays in biomedical applications.