Literature DB >> 19250815

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

Xin Huang1, Yanzhen Yin, Yang Liu, Xiaolong Bai, Zhiming Zhang, Jiayun Xu, Jiacong Shen, Junqiu Liu.   

Abstract

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.

Entities:  

Mesh:

Substances:

Year:  2009        PMID: 19250815     DOI: 10.1016/j.bios.2009.01.033

Source DB:  PubMed          Journal:  Biosens Bioelectron        ISSN: 0956-5663            Impact factor:   10.618


  2 in total

Review 1.  MIPs and Aptamers for Recognition of Proteins in Biomimetic Sensing.

Authors:  Marcus Menger; Aysu Yarman; Júlia Erdőssy; Huseyin Bekir Yildiz; Róbert E Gyurcsányi; Frieder W Scheller
Journal:  Biosensors (Basel)       Date:  2016-07-18

Review 2.  How Reliable Is the Electrochemical Readout of MIP Sensors?

Authors:  Aysu Yarman; Frieder W Scheller
Journal:  Sensors (Basel)       Date:  2020-05-08       Impact factor: 3.576

  2 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.