Home
This Title All WIREs
WIREs RSS Feed
How to cite this WIREs title:
WIREs Nanomed Nanobiotechnol
Impact Factor: 6.14

Protein‐protected metal nanoclusters: An emerging ultra‐small nanozyme

Full article on Wiley Online Library:   HTML PDF

Can't access this content? Tell your librarian.

Abstract Protein‐protected metal nanoclusters (MNCs), typically consisting of several to a hundred metal atoms with a protein outer layer used for protecting clusters from aggregation, are excellent fluorescent labels for biomedical applications due to their extraordinary photoluminescence, facile synthesis and good biocompatibility. Interestingly, many protein‐protected MNCs have also been reported to exhibit intrinsic enzyme‐like activities, namely peroxidase, oxidase and catalase activities, and are consequently used for biological analysis and environmental treatment. These findings have extended the horizon of protein‐protected MNCs' properties as well as their application in various fields. Furthermore, in the field of nanozymes, protein‐protected MNCs have emerged as an outstanding new addition. Due to their ultra‐small size (<2 nm), they usually have higher catalytic activity, more suitable size for in vivo application, better biocompatibility and photoluminescence in comparison with large size nanozymes. In this review, we will systematically introduce the significant advances in this field and critically discuss the challenges that lie ahead. Ultra‐small nanozymes based on protein‐protected MNCs are on the verge of attracting great interest across various disciplines and will stimulate research in the fields of nanotechnology and biology. This article is characterized under: Therapeutic Approaches and Drug Discovery > Emerging Technologies Biology‐Inspired Nanomaterials > Protein and Virus‐Based Structures
Protein as a protective ligand for the synthesis of MNCs. (a) Proteins are emerging as protective ligands for the synthesis of MNCs. (Reprinted with permission from Xavier, Chaudhari, Baksi, and Pradeep (). Copyright 2012 Taylor & Francis) (b) Schematic illustration of the formation of BSA‐protected Au NCs. (Reprinted with permission from Xie, Zheng, and Ying (). Copyright 2009 American Chemical Society)
[ Normal View | Magnified View ]
Catalase enzymatic activity of ferritin‐Ft NCs. (a) Schematic diagram of the synthesis method of Pt‐Ft. (b) The effects of catalase (i) and Pt‐Ft (ii) on H2O2/UV system. (c) Gas bubbles were observed in the quartz capillary tubes after the UV/H2O2 with catalase/Pt‐Ft experiment. (Reprinted with permission from J. Fan et al. (). Copyright 2011 Elsevier)
[ Normal View | Magnified View ]
Lys‐Pt NCs as an oxidase nanozyme and its application for degrading environmental pollutants. (a) Lys‐Pt NCs catalyze the oxidation of organic substrates such as TMB, ABTS and dopamine by O2. (b) Absorption spectra of oxidized ABTS catalyzed by Pt NCs under (a) N2 saturated and (b) aerobic conditions. (c) Absorption spectra of oxidized ABTS obtained in the absence (a) and presence of (b) Lys, (c) HRP, (d) 13 nm Au NPs, (e) 13 nm Fe3O4 NPs, (f) 30 nm Pt NPs, (g) 5 nm Pt NPs, and (h) Lys‐Pt NCs. (d) After the addition of Lys‐Pt NCs, the 665 nm maximal absorbance of methylene blue in lake water samples gradually decreases. (Reprinted with permission from C. J. Yu et al. (). Copyright 2014 Royal Society of Chemistry)
[ Normal View | Magnified View ]
Schematic diagram of the colorimetric detection of L. monocytogenes based on the oxidase activity of BSA‐Ag NCs. (a) GNPs aggregate in the presence of OPD. (b) The Ig Y‐BSA‐Ag NCs attached onto the sandwich‐type complex can catalyze the oxidization of OPD to ox‐OPD, which results in the disaggregation of GNPs. (Reprinted with permission from Liu et al. (). Copyright 2018 Springer‐Verlag GmbH Austria, part of Springer Nature)
[ Normal View | Magnified View ]
Oxidase nanozymes based on BSA‐Au NCs and its intriguing application. (a) The catalytic reaction mechanism of the photoactivated oxidase enzymatic activity of BSA‐Au NCs. (b) The colorimetric trypsin detection method based on the oxidase property of BSA‐Au NCs. (Reprinted with permission from G. L. Wang et al. (). Copyright 2015 Elsevier B.V.)
[ Normal View | Magnified View ]
The preparation of protein‐protected Cu NCs as peroxidase nanozymes and their application. (a) The scheme of stable BSA‐Cu NCs preparation. (Reprinted with permission from Yan et al. (). Copyright 2017 Springer Science Business Media) (b) Principle of the BSA‐Cu NCs‐based chemiluminescence sensor for cholesterol. (Reprinted with permission from Xu et al. (). Copyright 2016 Nature Publishing Group) (c, d) The fluorescence response of BSA‐Cu NC1 and BSA‐Cu NC2 toward different concentrations of dopamine. (Reprinted with permission from Aparna et al. (). Copyright 2019 Elsevier B.V.)
[ Normal View | Magnified View ]
Protective proteins provide different functions in protein‐protected MNCs nanozymes. (a) Prepared apoferritin‐paired gold clusters. (b) Stability of Au‐Ft and HRP. (Reprinted with permission from Jiang et al. (). Copyright 2015 Elsevier B.V.) (c) Formation of Au NCs at the threefold channel of apoferritin mutant. (Reprinted with permission from B. Maity, Abe, and Ueno (). Copyright 2017 Nature Publishing Group) (d) The colorimetric detection of Hg2+ using PRT‐Au NCs as a nanozyme. (Reprinted with permission from Y. Q. Huang et al. (). Copyright 2018 Springer‐Verlag GmbH Germany, part of Springer Nature) (e) Detection of free bilirubin by utilizing HSA‐Au NCs as a fluorometric and colorimetric probe. (Reprinted with permission from Santhosh et al. (). Copyright 2014 Elsevier B.V.)
[ Normal View | Magnified View ]
Detection methods based on the effect of substance on the peroxidase mimetic property of BSA‐Au NCs. (a) Schematic diagram of Hg2+ detection. (Reprinted with permission from Zhu et al. (). Copyright 2013 Elsevier B.V.) (b) Schematic diagram of the colorimetric detection of Cys and Hg2+ by BSA‐Au NCs. (Reprinted with permission from Y.‐W. Wang et al. (). Copyright 2016 Elsevier B.V.)
[ Normal View | Magnified View ]
Protein‐protected Au NCs as effective peroxidase nanozymes enhance CL of the luminol–H2O2 system. (a) CL kinetic curves of the luminol–H2O2–Au NCs system: (a) Au NCs; (b) luminol–H2O2; (c) luminol–H2O2–Au NCs. (Reprinted with permission from Deng et al. (). Copyright 2014 The Royal Society of Chemistry) (b) CL spectra of the luminol–H2O2 CL system: (a) H2O2 + luminol + cationic Au NCs; (b) H2O2 + luminol + Au NCs; (c) H2O2 + luminol + cationic BSA; (d) H2O2 + luminol + BSA; (e) H2O2 + luminol. (c) CL mechanisms of the luminol–H2O2 CL system catalyzed by cationic Au NCs. (Reprinted with permission from Han et al. (). Copyright 2018 John Wiley & Sons)
[ Normal View | Magnified View ]
Protein‐protected Au NCs as effective peroxidase nanozymes and the improvement of their catalytic activity. (a) BSA‐protected Au NCs exhibit peroxidase enzymatic activity. (Reprinted with permission from X. X. Wang et al. (). Copyright 2011 Elsevier B.V.) (b) MNPs‐Au NCs with enhanced peroxidase activity for the detection of glucose. (Reprinted with permission from Cho et al. (). Copyright 2017 AIP Publishing) (c) GO‐Au NCs with high peroxidase enzymatic activity over a wide pH range. (d) The target‐directed GO‐lysozyme‐Au NC hybrid used for cancer cell detection. (Reprinted with permission from Tao, Lin, Huang, et al. (). Copyright 2013 Wiley‐VCH Verlag GmbH & Co. KGaA)
[ Normal View | Magnified View ]

Browse by Topic

Biology-Inspired Nanomaterials > Protein and Virus-Based Structures
Therapeutic Approaches and Drug Discovery > Emerging Technologies

Access to this WIREs title is by subscription only.

Recommend to Your
Librarian Now!

The latest WIREs articles in your inbox

Sign Up for Article Alerts