The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Surface-Enhanced Raman Scattering Active Gold Nanoparticles with Enzyme-Mimicking Activities for Measuring Glucose and Lactate in Living Tissues
Abstract
Gold nanoparticles (AuNPs) with simultaneous plasmonic and biocatalytic properties provide a promising approach to developing versatile bioassays. However, the combination of AuNPs' intrinsic enzyme-mimicking properties with their surface-enhanced Raman scattering (SERS) activities has yet to be explored. Here we designed a peroxidase-mimicking nanozyme by in situ growing AuNPs into a highly porous and thermally stable metal-organic framework called MIL-101. The obtained AuNPs@MIL-101 nanozymes acted as peroxidase mimics to oxidize Raman-inactive reporter leucomalachite green into the active malachite green (MG) with hydrogen peroxide and simultaneously as the SERS substrates to enhance the Raman signals of the as-produced MG. We then assembled glucose oxidase (GOx) and lactate oxidase (LOx) onto AuNPs@MIL-101 to form AuNPs@MIL-101@GOx and AuNPs@MIL-101@LOx integrative nanozymes for in vitro detection of glucose and lactate via SERS. Moreover, the integrative nanozymes were further explored for monitoring the change of glucose and lactate in living brains, which are associated with ischemic stroke. The integrative nanozymes were then used to evaluate the therapeutic efficacy of potential drugs (such as astaxanthin for alleviating cerebral ischemic injuries) in living rats. They were also employed to determine glucose and lactate metabolism in tumors. This study not only demonstrated the great promise of combining AuNPs' multiple functionalities for versatile bioassays but also provided an interesting approach to designing nanozymes for biomedical and catalytic applications.
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Cites
Understanding the Warburg Effect: The Metabolic Requirements of Cell Proliferation
Vander Heiden, M. G., Cantley, L. C., & Thompson, C. B. (2009) · Science · doi:10.1126/science.1160809 · Cited by 16,197
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
Kong, K. V., Lam, Z., Lau, W. K. O., Leong, W. K., & Olivo, M. (2013) · Journal of the American Chemical Society · doi:10.1021/ja409230g · Cited by 173
Cited by
Immunomodulation‐Enhanced Nanozyme‐Based Tumor Catalytic Therapy
Xu, B., Cui, Y., Wang, W., Li, S., Lyu, C., Wang, S., Bao, W., Wang, H., Qin, M., Liu, Z., et al. (2020) · Advanced Materials · doi:10.1002/adma.202003563 · Cited by 404
Metal–organic framework based nanozymes: promising materials for biochemical analysis
Niu, X., Li, X., Lyu, Z., Pan, J., Ding, S., Ruan, X., Zhu, W., Du, D., & Lin, Y. (2020) · Chemical Communications · doi:10.1039/d0cc04890a · Cited by 328
Nitrogen-Doped Carbon Nanomaterials as Highly Active and Specific Peroxidase Mimics
Hu, Y., Gao, X. J., Zhu, Y., Muhammad, F., Tan, S., Cao, W., Lin, S., Jin, Z., Gao, X., & Wei, H. (2018) · Chemistry of Materials · doi:10.1021/acs.chemmater.8b02726 · Cited by 316
Self-citationMetal–Organic‐Framework‐Engineered Enzyme‐Mimetic Catalysts
Ma, L., Jiang, F., Fan, X., Wang, L., He, C., Zhou, M., Li, S., Luo, H., Cheng, C., & Qiu, L. (2020) · Advanced Materials · doi:10.1002/adma.202003065 · Cited by 298
Cheng, H., Liu, Y., Hu, Y., Ding, Y., Lin, S., Cao, W., Wang, Q., Wu, J., Muhammad, F., Zhao, X., et al. (2017) · Analytical Chemistry · doi:10.1021/acs.analchem.7b02895 · Cited by 267
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Metadata
- Authors
- Hu, Y., Cheng, H., Zhao, X., Wu, J., Muhammad, F., Lin, S., He, J., Zhou, L., Zhang, C., Deng, Y., Wang, P., Zhou, Z., Nie, S., & Wei, H.
- Venue
- ACS Nano
- Publisher
- American Chemical Society (ACS)
- Published
- 2017-06-01
- Volume
- 11
- Issue
- 6
- Pages
- 5558-5566
- ISSN
- 1936-0851 (ISSN-L)
- 1936-086X
- OpenAlex
- W2620153804
- Cited by
- 625
- References
- 3
- FWCI
- 29.47
- Type
- journal article
- Language
- en
- Open access
- closed
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