Journal article
Enzyme-mimic activity of ferric nano-core residing in ferritin and its biosensing applications
Analytical chemistry (Washington), Vol.83(22), pp.8611-8616
11/15/2011
Handle:
https://hdl.handle.net/2376/117061
PMID: 21910434
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.
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Details
- Title
- Enzyme-mimic activity of ferric nano-core residing in ferritin and its biosensing applications
- Creators
- Zhiwen Tang - Pacific Northwest National Laboratory, Richland, Washington 99352, United StatesHong WuYouyu ZhangZhaohui LiYuehe Lin
- Publication Details
- Analytical chemistry (Washington), Vol.83(22), pp.8611-8616
- Academic Unit
- Mechanical and Materials Engineering, School of
- Publisher
- United States
- Grant note
- U54 ES16015 / NIEHS NIH HHS
- Identifiers
- 99900547958301842
- Language
- English
- Resource Type
- Journal article