November 15, 2011
Journal Article

The Enzyme-mimic Activity of Ferric Nano-Core Residing in Ferritin and Its Biosensing Applications

Abstract

Ferritins are nano-scale 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 nano-core, 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 nano-biosensors, thus holds promising potential for facile and biocompatible labeling for sensitive and robust bioassays in biomedical applications.

Revised: December 13, 2011 | Published: November 15, 2011

Citation

Tang Z., H.J. Wu, Y. Zhang, Z. Li, and Y. Lin. 2011. The Enzyme-mimic Activity of Ferric Nano-Core Residing in Ferritin and Its Biosensing Applications. Analytical Chemistry 83, no. 22:8611–8616. PNNL-SA-81969. doi:10.1021/ac202049q