Exploiting cyclodextrins as artificial chaperones to enhance enzyme protection through supramolecular engineering

Type
01A - Journal article
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Parent work
Nanoscale
Special issue
DOI of the original publication
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Series
Series number
Volume
16
Issue / Number
10
Pages / Duration
5123-5129
Patent number
Publisher / Publishing institution
Royal Society of Chemistry
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Abstract
We report a method of enzyme stabilisation exploiting the artificial protein chaperone properties of β-cyclodextrin (β-CD) covalently embedded in an ultrathin organosilica layer. Putative interaction points of this artificial chaperone system with the surface of the selected enzyme were studied in silico using a protein energy landscape exploration simulation algorithm. We show that this enzyme shielding method allows for drastic enhancement of enzyme stability under thermal and chemical stress conditions, along with broadening the optimal temperature range of the biocatalyst. The presence of the β-CD macrocycle within the protective layer supports protein refolding after treatment with a surfactant.
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ISBN
ISSN
2040-3364
2040-3372
Language
English
Created during FHNW affiliation
Yes
Strategic action fields FHNW
Publication status
Published
Review
Peer review of the complete publication
Open access category
Hybrid
License
'https://creativecommons.org/licenses/by/4.0/'
Citation
Foroutan Kalourazi, A., Nazemi, S. A., Unniram Parambil, A. R., Muñoz-Tafalla, R., Vidal, P., Shahangian, S. S., Guallar, V., Ferrer, M., & Shahgaldian, P. (2024). Exploiting cyclodextrins as artificial chaperones to enhance enzyme protection through supramolecular engineering. Nanoscale, 16(10), 5123–5129. https://doi.org/10.1039/d3nr06044f