Reversible Switch of Artificial Selenoenzyme Activity Modulated by Metal Ion-Induced Protein Nano-Assemblies
Source abstract
Abstract
In this study, we used computational design and protein engineering to modify stabilizing protein 1 to mimic glutathione peroxidase (GPx), and constructed a reversible protein-assembled nanoscale artificial selenidase based on Ni 2+ -response. Its unique glutathione substrate recognition site and spatial orientation of the Se active center endow it with high GPx activity. The experimental results showed that the spatial barrier formed by Ni 2+ -induced assembly can inhibit enzyme activity, and EDTA can dissociate and restore activity. And the reversible protein assembly system is robust after multiple cycles, demonstrating the potential of this “intelligent” artificial selenoenzymatic nanomaterials for controllable catalytic applications in biomedicine.
Source: openalex_inverted_index · Quality: baseline
Research context
OpenAlex topics: Selenium in Biological Systems · Organoselenium and organotellurium chemistry · Redox biology and oxidative stress
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
Key Laboratory of Organosilicon Chemistry and Material Technology, Ministry of Education, College of Material, Chemistry and Chemical Engineering, Hangzhou Normal University, Hangzhou 311121, China
Funding
National Key Research and Development Program of China · National Natural Science Foundation of China · Interdisciplinary Research Project of Hangzhou Normal University · Hangzhou Leading Innovation and Entrepreneurship Team Project
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