Incorporation of glutathione peroxidase active site into polymer based on imprinting strategy

• Published in: Biosensors & bioelectronics Vol. 25; no. 3; pp. 657 - 660
• Main Authors: Huang, Xin, Yin, Yanzhen, Liu, Yang, Bai, Xiaolong, Zhang, Zhiming, Xu, Jiayun, Shen, Jiacong, Liu, Junqiu
• Format: Journal Article Conference Proceeding
• Language: English
• Published: Kidlington Elsevier B.V 15-11-2009; Elsevier
• Subjects: Artificial enzyme; Biological and medical sciences; Biosensing Techniques; Biotechnology; Catalytic Domain; Fundamental and applied biological sciences. Psychology; Glutathione - chemistry; Glutathione - metabolism; Glutathione peroxidase; Glutathione Peroxidase - chemistry; Glutathione Peroxidase - metabolism; Imprinting; Kinetics; Molecular Imprinting - methods; Polymer; Polymers - chemical synthesis; Polymers - chemistry; Glutathione peroxidase; Polymer; Imprinting; Artificial enzyme; Incorporation; Peroxidases; Enzyme; Active site; Oxidoreductases
• ISSN: 0956-5663; 1873-4235
• DOI: 10.1016/j.bios.2009.01.033

Glutathione peroxidase (GPx, EC 1.11.1.9) is a key enzyme involved in scavenging of reactive oxygen species in biological system. For developing an efficient GPx-like antioxidant, catalytically necessary amino acid derivatives which located near the GPx active center were prepared as functional monomers.
Via predetermined imprinting with substrate glutathione (GSH), a polymer-based GPx mimic with a similar structure of catalytic center of natural GPx was developed, and it demonstrated high-catalytic efficiency and substrate specificity. The imprinting polymer (
I-PEM) exhibits GPx-like activity about three times higher than that of 2-SeCD, a cyclodextrin-based GPx mimic. The detailed studies on kinetics revealed that not only the substrate binding but also positional arrangement of reacting groups contribute significantly to the catalytic efficiency of the peroxidase model.