The effect of WG-9 peptide on Glutathione peroxidase activity in human lung adenocarcinoma cell line (A549)

High amounts of reactive oxygen species (ROS) play a key role in human diseases like cancers. Nevertheless, several antioxidant enzymes such as superoxide dismutase, catalase, and glutathione peroxidase act to influence oxidative stress. Glutathione peroxidase (GPx) is an essential antioxidant enzyme that catalyzes the reduction of hydrogen peroxide, by reduced glutathione (GSH) and as same as other antioxidant enzymes, protects the cell from oxidative damage. In this study, we examined the activity of glutathione peroxidase in cultured cells treated with various concentration of WG-9 peptide for 24 h. we used UV spectrophotometer to determine the absorption of NADPH that reduced during the glutathione peroxidase system. Our results indicate the enzyme activity raises by increasing concentrations of the WG-9 peptide. The cytotoxicity effect of viable cells is measured through the MTT assay. Also, there is significant correlation between cytotoxicity of different concentrations of the peptide on cultured cancer cells.