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Reference type: Journal
Authors: Huang X, Liu Y, Liang K, Tang Y, Liu JQ
Article Title: Construction of the Active Site of Glutathione Peroxidase on Polymer-Based Nanoparticles.
Publication date: 2008
Journal: Biomacromolecules
Volume: 9
Issue: (5)
Page numbers: 1467-1473.
DOI: 10.1021/bm701386b

Abstract: Abstract: A new nanoenzyme model with glutathione peroxidase-like active site was constructed on polystyrene nanoparticle (PN1) via microemulsion polymerization. In this model system, two functional monomers were designed: one is a tellurium-containing compound that was introduced on the surface of the nanoparticle and acts as a catalytic center, and the other one is an arginine-containing compound designed as a binding site for the complexation of the carboxyl group of substrate 3-carboxy-4-nitrobenzenethiol (ArSH, 1). As a new glutathione peroxidase (GPx) mimic, it demonstrated excellent catalytic activity and substrate specificity. In ArSH assay system, it was at least 316000-fold more efficient than PhSeSePh for the reduction of cumene hydroperoxide (CUOOH) by ArSH. In contrast to model PN2, which lacks of substrate binding site, PN1 exhibits an obvious enhancement in catalytic activity. To further promote the catalytic efficiency, a substrate ArSH surface-imprinted nanoenzyme model (I-PN) was developed. By correctly incorporating and positioning the catalytic center tellurium and functional binding factor guanidinium, a continuative activity enhancement of 596000-fold for the reduction of CUOOH by catalyst I-PN compared with diphenyl diselenide (PhSeSePh) was observed. The results clearly show that polymeric nanoparticle can be developed as an excellent model for combining most of catalytic factors of enzyme into one scaffold
Template and target information: 3-carboxy-4-nitrobenzenethiol


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