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Artificial enzymes based on supramolecular scaffolds
Abstract
Enzymes are nanometer-sized molecules with three-dimensional structures created by the folding and self-assembly of polymeric chain-like components through supramolecular interactions. They are capable of performing catalytic functions usually accompanied by a variety of conformational states. The conformational diversities and complexities of natural enzymes exerted in catalysis seriously restrict the detailed understanding of enzymatic mechanisms in molecular terms. A supramolecular viewpoint is undoubtedly helpful in understanding the principle of enzyme catalysis. The emergence of supramolecular artificial enzymes therefore provides an alternative way to approach the structural complexity and thus to unravel the mystery of enzyme catalysis. This critical review covers the recent development of artificial enzymes designed based on supramolecular scaffolds ranging from the synthetic macrocycles to self-assembled nanometer-sized objects. Such findings are anticipated to facilitate the design of supramolecular artificial enzymes as well as their potential uses in important fields, such as manufacturing and food industries, environmental biosensors, pharmaceutics and so on.
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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
Dynamic personalities of proteins
Henzler-Wildman, K., & Kern, D. (2007) · Nature · doi:10.1038/nature06522 · Cited by 2,545
Cited by
Hu, P., Han, L., & Dong, S. (2014) · ACS Applied Materials & Interfaces · doi:10.1021/am404539j · Cited by 57
Metadata
- Authors
- Dong, Z., Luo, Q., & Liu, J.
- Venue
- Chemical Society Reviews
- Publisher
- Royal Society of Chemistry (RSC)
- Published
- 2012
- Volume
- 41
- Issue
- 23
- Pages
- 7890
- ISSN
- 0306-0012 (ISSN-L)
- 1460-4744
- OpenAlex
- W2089798763
- Cited by
- 402
- References
- 2
- FWCI
- 0.88
- Type
- journal article
- Language
- en
- Open access
- closed
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