title: Enzyme-mimic activity of ferric nano-core residing in ferritin and its biosensing applications.
abstract: 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.
authors.affiliation: Pacific Northwest National Laboratory, Richland, Washington 99352, United States.
authors.forename: Zhiwen
authors.initials: Z
authors.lastname: Tang
authors.forename: Hong
authors.initials: H
authors.lastname: Wu
authors.forename: Youyu
authors.initials: Y
authors.lastname: Zhang
authors.forename: Zhaohui
authors.initials: Z
authors.lastname: Li
authors.forename: Yuehe
authors.initials: Y
authors.lastname: Lin
mesh_terms: D015374:Biosensing Techniques; D005293:Ferritins / Q000737:chemistry* / Q000378:metabolism; D006735:Horseradish Peroxidase / Q000737:chemistry / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D018716:Molecular Mimicry; D053758:Nanoparticles / Q000737:chemistry*; D010316:Particle Size; D013499:Surface Properties; D013696:Temperature
chemical_list: D005293:Ferritins; D006735:Horseradish Peroxidase