Abstract
Glutathione peroxidase (GPx) is one of the most important antioxidative selenoenzymes in living organisms. The novel GPx mimic 6,6′-ditellurobis(6-deoxy-β-cyclodextrin) (6-TeCD) was prepared and evaluated for its capacity to catalyze the reduction of H2O2, tert-butyl hydroperoxide (t-BuOOH), and cumene hydroperoxide (CuOOH) by glutathione (GSH) or 3-carboxy-4-nitrobenzenethiol (ArSH). Compared the ArSH assay with the coupled reductase assay, we found that 6-TeCD exhibited strong substrate specificity for aromatic thiol substrate. The specificity led to efficient peroxidase activity almost 100,000-fold than that for a well-known GPx mimic diphenyl diselenide (PhSeSePh). Furthermore, reduction of lipophilic CuOOH was proceeded ca. 30 times faster than the more hydrophilic H2O2, which cannot bind into the hydrophobic cavity of β-cyclodextrin. Thus, it seemed that catalytic activity of cyclodextrin-derived GPx models strongly depends on the structurally different both substrates hydroperoxides (ROOH) and thiols.
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We are grateful to the financial support of the Natural Science Foundation of China (20534030, 20471023), Innovative Research Team in University (IRT0422), and the Ministry of Education of China.
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Dong, Z., Liu, J., Mao, S. et al. A Glutathione Peroxidase Mimic 6,6′-Ditellurobis (6-Deoxy-β-Cyclodextrin) with High Substrate Specificity. J Incl Phenom Macrocycl Chem 56, 179–182 (2006). https://doi.org/10.1007/s10847-006-9080-7
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DOI: https://doi.org/10.1007/s10847-006-9080-7