Surface Ligand Engineering Ruthenium Nanozyme Superior to Horseradish Peroxidase for Enhanced Immunoassay
© 2023 Wiley-VCH GmbH.
| Veröffentlicht in: | Advanced materials (Deerfield Beach, Fla.). - 1998. - 36(2024), 10 vom: 07. März, Seite e2300387 |
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| 1. Verfasser: | |
| Weitere Verfasser: | , , , , , , |
| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2024
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| Zugriff auf das übergeordnete Werk: | Advanced materials (Deerfield Beach, Fla.) |
| Schlagworte: | Journal Article Ru nanozymes enzyme-linked immunosorbent assay ligand modification peroxidase-like activity surface engineering Horseradish Peroxidase EC 1.11.1.- Ruthenium 7UI0TKC3U5 mehr... |
| Zusammenfassung: | © 2023 Wiley-VCH GmbH. Nanozymes have great potential to be used as an alternative to natural enzymes in a variety of fields. However, low catalytic activity compared with natural enzymes limits their practical use. It is still challenging to design nanozymes comparable to their natural counterparts in terms of the specific activity. In this study, a surface engineering strategy is employed to improve the specific activity of Ru nanozymes using charge-transferrable ligands such as polystyrene sulfonate (PSS). PSS-modified Ru nanozyme exhibits a peroxidase-like specific activity of up to 2820 U mg-1 , which is twice that of horseradish peroxidase (1305 U mg-1 ). Mechanism studies suggest that PSS readily accepts negative charge from Ru, thus reducing the affinity between Ru and ·OH. Importantly, the modified Ru-peroxidase nanozyme is successfully used to develop an immunoassay for human alpha-fetoprotein and achieves a 140-fold increase in detection sensitivity compared with traditional horseradish-peroxidase-based enzyme-linked immunosorbent assay. Therefore, this work provides a feasible route to design nanozymes with high specific activity that meets the practical use as an alternative to natural enzymes |
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| Beschreibung: | Date Completed 08.03.2024 Date Revised 08.03.2024 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1521-4095 |
| DOI: | 10.1002/adma.202300387 |