Abstract
Oxidative stress is implicated, either directly or indirectly, in the pathology of a range of human diseases. As a consequence, the development of efficient antioxidants for medical use has become increasingly important. Glutathione peroxidases (GPxs, EC 1.11.1.9) were first discovered in mammals as key enzymes involved in the scavenging of reactive oxygen species. Their efficient antioxidant activity depends on the presence of the rare amino acid residue selenocysteine (Sec) at the catalytic site. As intrinsic disadvantages of natural GPxs have limited their application, enormous efforts have been made to simulate the functions of GPx. Several strategies such as chemical synthesis, genetic engineering, catalytic antibodies, nanotechnology have been widely used. Herein, semisynthesized selenoproteins as GPx mimics have been mini-reviewed. Natural proteins have many intrinsic advantages for semisynthesis. Moreover, the semisynthesis method is easily manipulated with a relatively high yield and that is why it is increasingly applied at present.
| Original language | English |
|---|---|
| Title of host publication | Advanced Topics in Science and Technology in China |
| Publisher | Springer Science and Business Media Deutschland GmbH |
| Pages | 249-258 |
| Number of pages | 10 |
| DOIs | |
| State | Published - 2012 |
| Externally published | Yes |
Publication series
| Name | Advanced Topics in Science and Technology in China |
|---|---|
| ISSN (Print) | 1995-6819 |
| ISSN (Electronic) | 1995-6827 |
UN SDGs
This output contributes to the following UN Sustainable Development Goals (SDGs)
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SDG 3 Good Health and Well-being
Keywords
- Catalytic antibody
- Diphenyl diselenide
- Imprint molecule
- Selenenic acid
- Template molecule
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