Jilin University, Changchun, China.
J Microbiol Biotechnol. 2010 Jan;20(1):88-93.
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.
超氧化物歧化酶（SOD）、谷胱甘肽过氧化物酶（GPX）和过氧化氢酶（CAT）在平衡生物体内活性氧（ROS）的产生和分解方面发挥着关键作用。这些酶协同作用，共同清除 ROS。为了模拟这些酶的协同作用，我们在前 15 个具有 GPX 活性的肽和 17 个具有 SOD 活性的肽的基础上设计并合成了一种新型的 32 肽（32P）。在硒化和铜螯合作用下，32 肽转化为一种新的含有硒和铜的 32 肽（Se-Cu-32P），并具有 SOD 和 GPX 活性，并对其动力学进行了研究。此外，该新型肽比其亲本肽更能保护vero 细胞免受黄嘌呤氧化酶（XOD）/黄嘌呤/Fe2+损伤系统诱导的损伤。因此，这种双功能酶模拟了 SOD 和 GPX 的协同作用，可能成为一种更好的治疗药物候选物。
