Structural Analysis and Intrinsic Enzyme Mimicking Activities of Ligand-Free PtAg Nanoalloys

Nanozymes are nanomaterials with biocatalytic properties under physiological conditions and are one class of artificial enzymes to overcome the high cost and low stability of natural enzymes. However, surface ligands on nanomaterials will decrease the catalytic activity of the nanozymes by blocking...

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Main Authors: Bücker, R. (Author), Chakraborty, I. (Author), Chen, L. (Author), Gonzalez, M.G (Author), Klemeyer, L. (Author), Koeppen, A. (Author), Koziej, D. (Author), Liu, X. (Author), Parak, W.J (Author), Ruan, M. (Author), Werner, S. (Author), Xu, W. (Author)
Format: Article
Language:English
Published: John Wiley and Sons Inc 2023
Subjects:
Online Access:View Fulltext in Publisher
LEADER 03192nam a2200577Ia 4500
001 10.1002-smll.202206772
008 230526s2023 CNT 000 0 und d
020 |a 16136810 (ISSN) 
245 1 0 |a Structural Analysis and Intrinsic Enzyme Mimicking Activities of Ligand-Free PtAg Nanoalloys 
260 0 |b John Wiley and Sons Inc  |c 2023 
856 |z View Fulltext in Publisher  |u https://doi.org/10.1002/smll.202206772 
520 3 |a Nanozymes are nanomaterials with biocatalytic properties under physiological conditions and are one class of artificial enzymes to overcome the high cost and low stability of natural enzymes. However, surface ligands on nanomaterials will decrease the catalytic activity of the nanozymes by blocking the active sites. To address this limitation, ligand-free PtAg nanoclusters (NCs) are synthesized and applied as nanozymes for various enzyme-mimicking reactions. By taking advantage of the mutual interaction of zeolitic imidazolate frameworks (ZIF-8) and Pt precursors, a good dispersion of PtAg bimetal NCs with a diameter of 1.78 ± 0.1 nm is achieved with ZIF-8 as a template. The incorporation of PtAgNCs in the voids of ZIF-8 is confirmed with structural analysis using the atomic pair-distribution function and powder X-ray diffraction. Importantly, the PtAgNCs present good catalytic activity for various enzyme-mimicking reactions, including peroxidase-/catalase- and oxidase-like reactions. Further, this work compares the catalytic activity between PtAg NCs and PtAg nanoparticles with different compositions and finds that these two nanozymes present a converse dependency of Ag-loading on their activity. This study contributes to the field of nanozymes and presents a potential option to prepare ligand-free bimetal biocatalysts with sizes in the nanocluster regime. © 2023 The Authors. Small published by Wiley-VCH GmbH. 
650 0 4 |a Artificial enzymes 
650 0 4 |a Bimetals 
650 0 4 |a Binary alloys 
650 0 4 |a Biocatalytic properties 
650 0 4 |a Catalyst activity 
650 0 4 |a Enzyme activity 
650 0 4 |a Enzyme mimicing 
650 0 4 |a enzyme mimicking 
650 0 4 |a High costs 
650 0 4 |a High-low 
650 0 4 |a Ligand-free 
650 0 4 |a Ligands 
650 0 4 |a nanoalloys 
650 0 4 |a Nano-alloys 
650 0 4 |a nanoclusters 
650 0 4 |a Nanoclusters 
650 0 4 |a nanoparticles 
650 0 4 |a Nanoparticles 
650 0 4 |a Nanostructured materials 
650 0 4 |a Pair distribution functions 
650 0 4 |a pair-distribution function 
650 0 4 |a Physiological condition 
650 0 4 |a Powder X-ray diffraction analyse 
650 0 4 |a powder X-ray diffraction analysis 
650 0 4 |a Structural analysis 
650 0 4 |a X ray powder diffraction 
700 1 0 |a Bücker, R.  |e author 
700 1 0 |a Chakraborty, I.  |e author 
700 1 0 |a Chen, L.  |e author 
700 1 0 |a Gonzalez, M.G.  |e author 
700 1 0 |a Klemeyer, L.  |e author 
700 1 0 |a Koeppen, A.  |e author 
700 1 0 |a Koziej, D.  |e author 
700 1 0 |a Liu, X.  |e author 
700 1 0 |a Parak, W.J.  |e author 
700 1 0 |a Ruan, M.  |e author 
700 1 0 |a Werner, S.  |e author 
700 1 0 |a Xu, W.  |e author 
773 |t Small  |x 16136810 (ISSN)  |g 19 19