The DOI matches its Crossref record; 38 of the 38 references it cites were found in a registry or an index.
Co3O4 Nanoparticles with Multi-Enzyme Activities and Their Application in Immunohistochemical Assay
Abstract
Co3O4 nanoparticles (Co3O4 NPs), synthesized by the coprecipitation method, showed intrinsic catalase-like, peroxidase-like, and SOD-like activity. The catalytic activity of Co3O4 NPs was much higher than analogous Fe3O4 NPs. Co3O4's mechanisms of catalytic activity were analyzed in detail using the electron spin resonance (ESR) method, which confirmed that Co3O4 NPs don't follow the classical Fenton reactions with hydrogen peroxide the way Fe3O4 NPs do. The high redox potential of Co(3+)/Co(2+) was supposed to be the leading cause of the differences in both activity and mechanism with Fe3O4. Based on the high, peroxidase-like activity, a new immunohistochemical assay was designed in which the avastin antibody was conjugated onto the surface of Co3O4 NPs. The conjugates obtained were used to detect vascular endothelial growth factor (VEGF) that was overexpressed in tumor tissue. When the experimental and control groups were stained, there were clear distinctions between them. This study showed that there are many opportunities to improve the enzyme-like activities of nanomaterials and also to improve their potential applications for biocatalysis and bioassays, especially in relatively harsh conditions.
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Citations
Cites
The biology of VEGF and its receptors
Ferrara, N., Gerber, H.-P., & LeCouter, J. (2003) · Nature Medicine · doi:10.1038/nm0603-669 · Cited by 9,591
Intrinsic peroxidase-like activity of ferromagnetic nanoparticles
Gao, L., Zhuang, J., Nie, L., Zhang, J., Zhang, Y., Gu, N., Wang, T., Feng, J., Yang, D., Perrett, S., et al. (2007) · Nature Nanotechnology · doi:10.1038/nnano.2007.260 · Cited by 7,483
Self-citationVascular Endothelial Growth Factor: Basic Science and Clinical Progress
Ferrara, N. (2004) · Endocrine Reviews · doi:10.1210/er.2003-0027 · Cited by 3,687
LXXIII.—Oxidation of tartaric acid in presence of iron
Fenton, H. J. H. (1894) · J. Chem. Soc., Trans. · doi:10.1039/ct8946500899 · Cited by 3,179
Low-temperature oxidation of CO catalysed by Co3O4 nanorods
Xie, X., Li, Y., Liu, Z.-Q., Haruta, M., & Shen, W. (2009) · Nature · doi:10.1038/nature07877 · Cited by 2,622
Mesoporous Co3O4Nanowire Arrays for Lithium Ion Batteries with High Capacity and Rate Capability
Li, Y., Tan, B., & Wu, Y. (2008) · Nano Letters · doi:10.1021/nl0725906 · Cited by 1,271
Self-citationCo3O4 Nanomaterials in Lithium‐Ion Batteries and Gas Sensors
Li, W. Y., Xu, L. N., & Chen, J. (2005) · Advanced Functional Materials · doi:10.1002/adfm.200400429 · Cited by 1,201
Lou, X. W., Deng, D., Lee, J. Y., Feng, J., & Archer, L. A. (2008) · Advanced Materials · doi:10.1002/adma.200702412 · Cited by 1,014
Bevacizumab (Avastin), a humanized anti-VEGF monoclonal antibody for cancer therapy
Ferrara, N., Hillan, K. J., & Novotny, W. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.05.132 · Cited by 977
Hu, L., Peng, Q., & Li, Y. (2008) · Journal of the American Chemical Society · doi:10.1021/ja806400e · Cited by 948
Chen, Z., Yin, J.-J., Zhou, Y.-T., Zhang, Y., Song, L., Song, M., Hu, S., & Gu, N. (2012) · ACS Nano · doi:10.1021/nn300291r · Cited by 940
Self-citationTumor refractoriness to anti-VEGF treatment is mediated by CD11b+Gr1+ myeloid cells
Shojaei, F., Wu, X., Malik, A. K., Zhong, C., Baldwin, M. E., Schanz, S., Fuh, G., Gerber, H.-P., & Ferrara, N. (2007) · Nature Biotechnology · doi:10.1038/nbt1323 · Cited by 849
Rationally designed nanostructures for surface-enhanced Raman spectroscopy
Banholzer, M. J., Millstone, J. E., Qin, L., & Mirkin, C. A. (2008) · Chemical Society Reviews · doi:10.1039/b710915f · Cited by 795
Intrinsic peroxidase-like activity and catalase-like activity of Co3O4 nanoparticles
Mu, J., Wang, Y., Zhao, M., & Zhang, L. (2012) · Chemical Communications · doi:10.1039/c2cc17013b · Cited by 768
Wiechelman, K. J., Braun, R. D., & Fitzpatrick, J. D. (1988) · Analytical Biochemistry · doi:10.1016/0003-2697(88)90383-1 · Cited by 766
Au@Pt nanostructures as oxidase and peroxidase mimetics for use in immunoassays
He, W., Liu, Y., Yuan, J., Yin, J.-J., Wu, X., Hu, X., Zhang, K., Liu, J., Chen, C., Ji, Y., et al. (2011) · Biomaterials · doi:10.1016/j.biomaterials.2010.09.040 · Cited by 587
Self-citationDirect evidence for catalase and peroxidase activities of ferritin–platinum nanoparticles
Fan, J., Yin, J.-J., Ning, B., Wu, X., Hu, Y., Ferrari, M., Anderson, G. J., Wei, J., Zhao, Y., & Nie, G. (2011) · Biomaterials · doi:10.1016/j.biomaterials.2010.11.004 · Cited by 488
Self-citationZhao, H., Joseph, J., Zhang, H., Karoui, H., & Kalyanaraman, B. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00619-0 · Cited by 402
Prussian blue modified iron oxide magnetic nanoparticles and their high peroxidase-like activity
Zhang, X.-Q., Gong, S.-W., Zhang, Y., Yang, T., Wang, C.-Y., & Gu, N. (2010) · Journal of Materials Chemistry · doi:10.1039/c0jm00174k · Cited by 382
Self-citationVoinov, M. A., Pagán, J. O. S., Morrison, E., Smirnova, T. I., & Smirnov, A. I. (2011) · Journal of the American Chemical Society · doi:10.1021/ja104683w · Cited by 372
Novel Fluorometric Assay for Hydroxyl Radical Prevention Capacity Using Fluorescein as the Probe
Ou, B., Hampsch-Woodill, M., Flanagan, J., Deemer, E. K., Prior, R. L., & Huang, D. (2002) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf011480w · Cited by 349
Yu, F., Huang, Y., Cole, A. J., & Yang, V. C. (2009) · Biomaterials · doi:10.1016/j.biomaterials.2009.05.005 · Cited by 308
Structural Effects of Fe3O4 Nanocrystals on Peroxidase‐Like Activity
Liu, S., Lu, F., Xing, R., & Zhu, J. (2011) · Chemistry – A European Journal · doi:10.1002/chem.201001789 · Cited by 267
Dong, Y., He, K., Yin, L., & Zhang, A. (2007) · Nanotechnology · doi:10.1088/0957-4484/18/43/435602 · Cited by 262
Cobalt-mediated generation of reactive oxygen species and its possible mechanism
Leonard, S., M. Gannett, P., Rojanasakul, Y., Schwegler-Berry, D., Castranova, V., Vallyathan, V., & Shi, X. (1998) · Journal of Inorganic Biochemistry · doi:10.1016/s0162-0134(98)10022-3 · Cited by 209
Perez, J. M. (2007) · Nature Nanotechnology · doi:10.1038/nnano.2007.282 · Cited by 160
Stolze, K., Udilova, N., & Nohl, H. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00401-9 · Cited by 137
Layered Titanate Nanosheets Intercalated with Myoglobin for Direct Electrochemistry
Zhang, L., Zhang, Q., & Li, J. (2007) · Advanced Functional Materials · doi:10.1002/adfm.200600991 · Cited by 118
Mate, V. R., Shirai, M., & Rode, C. V. (2012) · Catalysis Communications · doi:10.1016/j.catcom.2012.12.015 · Cited by 104
Klem, M. T., Resnick, D. A., Gilmore, K., Young, M., Idzerda, Y. U., & Douglas, T. (2007) · Journal of the American Chemical Society · doi:10.1021/ja0667561 · Cited by 101
Size-dependent peroxidase-like catalytic activity of Fe3O4 nanoparticles
Peng, F. F., Zhang, Y., & Gu, N. (2008) · Chinese Chemical Letters · doi:10.1016/j.cclet.2008.03.021 · Cited by 98
Self-citationVerma, P., Baldrián, P., & Nerud, F. (2003) · Chemosphere · doi:10.1016/s0045-6535(02)00705-1 · Cited by 90
A comparison of cobalt(II) and iron(II) hydroxyl and superoxide free radical formation
Kadiiska, M. B., Maples, K. R., & Mason, R. P. (1989) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(89)90354-8 · Cited by 88
Jönsson, M., Lind, J., Reitberger, T., Eriksen, T. E., & Merényi, G. (1993) · The Journal of Physical Chemistry · doi:10.1021/j100145a027 · Cited by 81
Oxygen-derived free-radical and active oxygen complex formation from cobalt(II) chelates in vitro
Hanna, P. M., Kadiiska, M. B., & Mason, R. P. (1992) · Chemical Research in Toxicology · doi:10.1021/tx00025a019 · Cited by 79
Nanoparticulate Peroxidase/Catalase Mimetic and Its Application
Deng, H., Shen, W., Peng, Y., Chen, X., Yi, G., & Gao, Z. (2012) · Chemistry - A European Journal · doi:10.1002/chem.201200643 · Cited by 75
Ultra-small particles of iron oxide as peroxidase for immunohistochemical detection
Wu, Y., Song, M., Xin, Z., Zhang, X., Zhang, Y., Wang, C., Li, S., & Gu, N. (2011) · Nanotechnology · doi:10.1088/0957-4484/22/22/225703 · Cited by 58
Self-citationOne-Electron Reduction Potential of the Neutral Guanyl Radical in the GC Base Pair of Duplex DNA
Shinde, S. S., Maroz, A., Hay, M. P., & Anderson, R. F. (2009) · Journal of the American Chemical Society · doi:10.1021/ja8087339 · Cited by 42
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Nanomaterials with enzyme-like characteristics (nanozymes): next-generation artificial enzymes
Wei, H., & Wang, E. (2013) · Chemical Society Reviews · doi:10.1039/c3cs35486e · Cited by 3,779
Jomova, K., Alomar, S. Y., Alwasel, S. H., Nepovimova, E., Kuca, K., & Valko, M. (2024) · Archives of Toxicology · doi:10.1007/s00204-024-03696-4 · Cited by 1,445
Standardized assays for determining the catalytic activity and kinetics of peroxidase-like nanozymes
Jiang, B., Duan, D., Gao, L., Zhou, M., Fan, K., Tang, Y., Xi, J., Bi, Y., Tong, Z., Gao, G. F., et al. (2018) · Nature Protocols · doi:10.1038/s41596-018-0001-1 · Cited by 1,300
Singh, N., Savanur, M. A., Srivastava, S., D'Silva, P., & Mugesh, G. (2017) · Angewandte Chemie International Edition · doi:10.1002/anie.201708573 · Cited by 657
Surface modification of nanozymes
Liu, B., & Liu, J. (2017) · Nano Research · doi:10.1007/s12274-017-1426-5 · Cited by 543
Metadata
- Authors
- Dong, J., Song, L., Yin, J.-J., He, W., Wu, Y., Gu, N., & Zhang, Y.
- Venue
- ACS Applied Materials & Interfaces
- Publisher
- American Chemical Society (ACS)
- Published
- 2014-01-13
- Volume
- 6
- Issue
- 3
- Pages
- 1959-1970
- ISSN
- 1944-8244 (ISSN-L)
- 1944-8252
- OpenAlex
- W2139046196
- Cited by
- 454
- References
- 38
- FWCI
- 9.38
- Type
- journal article
- Language
- en
- Open access
- closed
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