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Catalysts 2017, 7(10), 289; doi:10.3390/catal7100289

Study of 8 Types of Glutathione Peroxidase Mimics Based on β-Cyclodextrin

,
,
and
*
Key Laborabory for Molecular Enzymology and Engineering of the Ministry of Education, Jilin University, Changchun 130023, China
These authors contributed equally to this work.
*
Author to whom correspondence should be addressed.
Received: 15 September 2017 / Revised: 25 September 2017 / Accepted: 26 September 2017 / Published: 28 September 2017
(This article belongs to the Special Issue Biocatalysis and Biotransformations)
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Abstract

Glutathione peroxidase is key for the removal of H2O2 and other hydroperoxides and therefore, it has an important role in the maintenance of the reactive oxygen species (ROS) metabolic balance in vivo. The native enzymes of the glutathione peroxidase family (GPx) have many defects, such as instability in vitro and poor availability. GPx mimetics has become a topic of considerable interest in artificial enzyme research. Many forms of GPx mimics have been synthesized, by including selenium and tellurium (double-bridged and single-bridged, 2-substituted and 6-substituted) in a mother molecule but differences the GPx mimics enzymatic activity have rarely been compared. We designed and synthesized eight cyclodextrin derivatives and used two types of enzyme assays to determine their activities. The results show that: (a) tellurium-containing GPx mimics have higher activity than that of selenium-containing GPx mimics; (b) dual-bridged mimics have higher activity than bis-bridged mimics; and (c) 2-position modified cyclodextrin has higher activity than 6-position modified cyclodextrin. View Full-Text
Keywords: glutathione peroxidase; mimic enzyme; cyclodextrin derivatives; enzyme activity; kinetics glutathione peroxidase; mimic enzyme; cyclodextrin derivatives; enzyme activity; kinetics
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Wang, L.; Qu, X.; Xie, Y.; Lv, S. Study of 8 Types of Glutathione Peroxidase Mimics Based on β-Cyclodextrin. Catalysts 2017, 7, 289.

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