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

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.

Keywords

Subject (DDC)

500 - Naturwissenschaften und Mathematik

Project

Event

Exhibition start date

Exhibition end date

Conference start date

Conference end date

Date of the last check

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

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

Full item page