A smart artificial glutathione peroxidase with temperature responsive activity constructed by host–guest interaction and self-assembly
| Autor: | Chao Lang, Junqiu Liu, Yanzhen Yin, Shufei Jiao |
|---|---|
| Rok vydání: | 2014 |
| Předmět: |
chemistry.chemical_classification
General Chemical Engineering Glutathione peroxidase technology industry and agriculture Supramolecular chemistry macromolecular substances General Chemistry Polymer Combinatorial chemistry Catalysis Enzyme catalysis chemistry Organic chemistry Molecule Enzyme kinetics Self-assembly |
| Zdroj: | RSC Adv.. 4:25040-25050 |
| ISSN: | 2046-2069 |
| DOI: | 10.1039/c4ra04042b |
| Popis: | A smart supramolecular artificial glutathione peroxidase (GPx) with tunable catalytic activity was prepared based on host–guest interaction and a blending process. The functional guest molecules ADA-Te with catalytic center, ADA-Arg with binding site and the cyclodextrin-containing host polymers (CD-PNIPAMs) were first synthesized. The artificial glutathione peroxidase was constructed by host–guest interaction of ADA-Te and a series of CD-PNIPAMs with different molecular weights. Through altering the molar ratio of building blocks (CD-PNIPAM73, ADA-Te, ADA-Arg), the optimum artificial GPx (SGPxmax) with vesicle structure was prepared via a blending process. Significantly, SGPxmax displayed a noticeable temperature responsive catalytic activity and exhibited typical saturation kinetics behavior of a real enzyme catalyst. It was proved that the change of the self-assembled structure of SGPxmax during the temperature responsive process played a significant role in altering the temperature responsive catalytic behavior. The construction of SGPxmax not only overcomes the insurmountable disadvantages existing in traditional supramolecular artificial GPxs but also bodes well for development of other biologically related functional supramolecular biomaterials. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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