A Compartmentalized Nanoreactor Formed by Interfacial Hydrogelation for Cascade Enzyme Catalytic Therapy. Issue 15 (2nd March 2023)

• Record Type: Journal Article
• Authors: He, Xingyue; Wu, Qing; Hou, Chen; Hu, Min; Wang, Qigang; Wang, Xia
• Is Part Of: Angewandte Chemie international edition. Volume 62:Issue 15(2023)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2023-03-02
• Subjects: Cascade Catalysis -- Enzymatic Hydrogelation -- Interfacial Functionalization -- Tumor Therapy; Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.202218766
• Languages: English
• ISSNs: 1433-7851

Abstract

Abstract: Some cellular enzymatic pathways are located within a single organelle, while most others involve enzymes that are located within multiple compartmentalized cellular organelles to realize the efficient multi‐step enzymatic process. Herein, bioinspired by enzyme‐mediated biosynthesis and biochemical defense, a compartmented nanoreactor (Burr‐NCs@Gl SOD ) was constructed through a self‐confined catalysis strategy with burr defect‐engineered molybdenum disulfide/Prussian blue analogues (MoS2 /PBA) and an interfacial diffusion‐controlled hydrogel network. The specific catalytic mechanism of the laccase‐like superactivity induced hydrogelation and cascade enzyme catalytic therapy were explored. The confined hydrogelation strategy introduces a versatile means for nanointerface functionalization and provides insight into biological construction of simulated enzymes with comparable activity and also the specificity to natural enzymes. Abstract : The compartmented Burr‐NCs@Gl SOD nanoreactor was constructed by a self‐confined catalysis strategy. The specific catalytic mechanism of the laccase‐like superactivity induced hydrogelation and core–shell cascade laccase‐SOD and SOD‐Fenton catalytic therapy were explored. The work introduces a versatile means for nanointerface functionalization and biological construction of simulated enzymes with comparable activity and specificity to natural enzymes.