A Novel Selenium- and Copper-Containing Peptide with Both Superoxide Dismutase and Glutathione Peroxidase Activities

• Published in: Journal of microbiology and biotechnology Vol. 20; no. 1; pp. 88 - 93
• Main Authors: Zou, Xian-Feng, Ji, Yue-Tong, Gao, Gui, Zhu, Xue-Jun, Lv, Shao-Wu, Yan, Fei, Han, Si-Ping, Chen, Xing, Gao, Chang-Cheng, Liu, Jun-Qiu, Luo, Gui-Min
• Format: Journal Article
• Language: Korean
• Published: 한국미생물생명공학회 30.01.2010
• Subjects: bifunctional enzyme; glutathione peroxidase; reactive oxygen species; Superoxide dismutase; synergism; synergism; Superoxide dismutase; bifunctional enzyme; reactive oxygen species; glutathione peroxidase
• ISSN: 1017-7825; 1738-8872

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 was converted to a new Se- and Cu-containing 32-mer peptide (Se-Cu-32P) that displayed 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 the xanthine oxidase (XOD)/xanthine/$Fe^{2+}$ 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.