| Literature DB >> 11933237 |
Xiaojun Ren1, Yan Xue, Junqiu Liu, Kun Zhang, Jian Zheng, Guimin Luo, Canhui Guo, Ying Mu, Jiacong Shen.
Abstract
A novel dicyclodextrinyl ditelluride (2-TeCD) compound was devised as a functional mimic of the glutathione peroxidase (GPX) enzymes that normally remove hydroperoxides from the cell. The GPX activity of the mimic was found to be 46.7 U microM(-1), which is 46 times as active as Ebselen, a well-known GPX mimic. A detailed steady-state kinetic study was undertaken to probe the reason for the high catalytic efficiency of 2-TeCD. This high efficiency can be explained based on both the binding of the substrate to the cyclodextrin and the catalytic mechanism of 2-TeCD, which is different from that of diselenide compounds. 2-TeCD exhibits good water solubility and is chemically and biologically stable. The biological effect of 2-TeCD was evaluated by its ability to protect mitochondria from oxidative damage. 2-TeCD exhibited excellent antioxidant capacity in comparison with Ebselen.Entities:
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Year: 2002 PMID: 11933237 DOI: 10.1002/1439-7633(20020402)3:4<356::AID-CBIC356>3.0.CO;2-O
Source DB: PubMed Journal: Chembiochem ISSN: 1439-4227 Impact factor: 3.164