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KMID : 0545120100200010088
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Journal of Microbiology and Biotechnology
2010 Volume.20 No. 1 p.88 ~ p.93
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A Novel Selenium and Copper-containing Peptide with Both Superoxide Dismutase and Glutathione Peroxidase Activities
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Zou Xian-Feng
Ji Yue-Tong
Gao Gui
Zhu Xue-Jun
Lv Shao-Wu
Yan Fei
Han Si-Ping
Luo Gui-Min
Chen Xing
Gao Chang-Cheng
Liu Jun-Qiu
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Abstract
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Superoxide dismutase (SOD), glutathione peroxidase (GPX) and catalase (CAT) play crucial roles in balancing the production and decomposition of reactive oxygen species (ROS) in living organisms. These enzymes act cooperatively and synergistically to scavenge ROS. In order to imitate the synergism of these enzymes, we designed and synthesized a novel 32-mer peptide (32P) on the basis of the previous 15-mer peptide with GPX activity and a 17-mer peptide with SOD activity. Upon the selenation and chelation of copper, the 32-mer peptide is converted to a new Se- and Cu-containing 32-mer peptide (Se-Cu-32P) and displays both SOD and GPX activities and its kinetics was studied. Moreover, the novel peptide was demonstrated to be able to better protect vero cells from the injury induced by xanthine oxidase (XOD)/xanthine/Fe2+ damage system than its parents. Thus, this bifunctional enzyme imitated the synergism of SOD and GPX and could be a better candidate of therapeutic medicine.
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KEYWORD
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superoxide dismutase, glutathione peroxidase, bifunctional enzyme, reactive oxygen species, synergism
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