Issue 10, 2024

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

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.

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

Supplementary files

Article information

Article type
Communication
Submitted
28 Nov 2023
Accepted
06 Feb 2024
First published
13 Feb 2024
This article is Open Access
Creative Commons BY license

Nanoscale, 2024,16, 5123-5129

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

A. Foroutan Kalourazi, S. A. Nazemi, A. R. Unniram Parambil, R. Muñoz-Tafalla, P. Vidal, S. S. Shahangian, V. Guallar, M. Ferrer and P. Shahgaldian, Nanoscale, 2024, 16, 5123 DOI: 10.1039/D3NR06044F

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