\”German Applied Chemistry\” reported Tongji Wang Qigang team of \”artificial multi-enzyme\”
Most of the enzyme is commonly nano metal compound nanoparticles, catalytic activity is mainly derived from the metal ions in the nano particle surface. In nature, characterized enzyme active site and indicates support, stabilize the active site of a network environment is also important for high catalytic efficiency. We can achieve high activity and selectivity by adjusting the composition and the active site environment. Hydrogels are a class of three-dimensional network of hydrophilic material with good biocompatibility, which can effectively protect the structure of the active center of the enzyme molecules, while providing a better substrate for migration microenvironment, thereby achieving efficient catalysis, the enzyme carrier the hydrogel material has become the focus of biological research. Nanogel a nanoparticle hydrogels, hydrophilic network having transmission characteristics and the like similar to the macroscopic fluid hydrogel material, which nano-size can be used as a carrier over a further in vivo biological applications. In the limited space in the realization of nano-modified or assembled in order to obtain nano-gel hybrid remains a challenge. In view of this, Tongji Wang Qigang team From the perspective of biomimetic, designed an enzyme-catalyzed atom transfer radical polymerization (ATRPase) and metal complex cross-linking method artificial nano successfully prepared multi-enzyme gel system. The simulation system having superoxide dismutase (SOD-like) and peroxidase (POD-like) properties, may be achieved in response to the imaging of the tumor microenvironment cascade catalysis. The research results \”Multienzyme-Mimic Nanogels Synthesized by Biocatalytic ATRP and Metal Coordination for Bioresponsive Fluorescence Imaging\” in the title, published in the internationally renowned academic journal Angewandte Chemie International Edition. The only communication Author Chemistry, Tongji University School of Science and Engineering thesis, master\’s Tongji University Simmel Park as the first author School of Chemical Science and Engineering Professor Wang Xiafu and Wang Qigang Professor as a co-corresponding author. Researchers first modified enzyme catalysed surface of the nanoparticles atom transfer radical polymerization initiator (-Br), in order to have good biocompatibility enzyme catalyst, double bond modified lysine (N-acryloyl-L-lysine) as a polymerizable monomer, polymerization of the nanoparticles around polylysine prepared polymer brushes, the final ligands crosslinked by ferrous, issued how to construct an artificial multi-enzyme activity gel system (Figure 1). Gel system, Fe ions highly dispersed gel network as a crosslinking agent on the one hand, while analog as an active center of the enzyme. And by POD and SOD analog, high levels of tumor site first O2 • – the catalytic conversion of H2O2, further lifting of the H2O2 based on the tumor site for secure tumor microenvironment cascade response by enzyme-catalyzed reaction, efficient tumor imaging. The plurality of artificial enzyme gel system similar natural peroxidase-catalyzed mechanism does not generate hydroxyl radicals, having low toxicity and high biosafety. Meanwhile, ATRPase method and metal complex crosslinking technology may be prepared by a variety of nanomaterials further achieved systems for drug delivery and other biomedical applications.
The research was funded by the National Natural Science Support Foundation, and other key national research and development program as well as the strong support of the Ministry of Science Center of the Chinese Academy of Sciences magnetic field. Professor Wang Qigang team has been committed to the polymer gel immobilized enzyme technology and bio-medical applications, the past five years to a total of Correspondence Adv.Mater in ., Nat. Commun., Angew. Chem. Inter. Ed. and other SCI journals published more than 50 papers. Document link: https: //www.onlinelibrary.wiley.com/doi/abs/10.1002/anie.202002331 Task Force Web site: https: //qgwang.tongji.edu.cn/