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Modulating the catalytic activity of gold nanoparticles using amine-terminated ligands
Nanozymes have broad applications in theranostics and point-of-care tests. To enhance the catalytic activity of nanozymes, the conventional strategy is doping metals to form highly active nanoalloys. However, high-quality and stable nanoalloys are hard to synthesize. Ligand modification is a powerfu...
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Published in: | Chemical science (Cambridge) 2022-01, Vol.13 (4), p.18-187 |
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Main Authors: | , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | Nanozymes have broad applications in theranostics and point-of-care tests. To enhance the catalytic activity of nanozymes, the conventional strategy is doping metals to form highly active nanoalloys. However, high-quality and stable nanoalloys are hard to synthesize. Ligand modification is a powerful strategy to achieve chemoselectivity or bioactivity by changing the surface chemistry. Here, we explore different ligands to enhance the catalytic activity of nanozymes,
e.g.
, gold nanoparticles (AuNPs). We systematically studied the impacts on the enzymatic activity of AuNPs by ligand engineering of surface chemistry (charge, group, and surface distance). Our work established critical guidelines for surface modification of nanozymes. The amine group favors higher activity of AuNPs than other groups. The flexible amine-rich ligand enhances the catalytic activity of AuNPs in contrast to other ligands and unmodified AuNPs. Using a proof-of-concept model, we screened many candidate ligands to obtain polyamine-AuNPs, which have strongly enhanced peroxidase-like activity and 100 times enhanced sensitivity compared to unmodified AuNPs. The strategy of enhancing the catalytic activity of AuNPs using ligands will facilitate the catalysis-related applications of nanozymes in biology and diagnostics.
Surface ligand engineering can precisely modulate the catalytic activity of nanozymes from inactive to highly active. |
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ISSN: | 2041-6520 2041-6539 |
DOI: | 10.1039/d1sc05933e |