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.

Schlagwörter

Fachgebiet (DDC)

500 - Naturwissenschaften und Mathematik

Projekt

Veranstaltung

Startdatum der Ausstellung

Enddatum der Ausstellung

Startdatum der Konferenz

Enddatum der Konferenz

Datum der letzten Prüfung

ISBN

ISSN

2040-3364
2040-3372

Sprache

Englisch

Während FHNW Zugehörigkeit erstellt

Ja

Zukunftsfelder FHNW

Publikationsstatus

Veröffentlicht

Begutachtung

Peer-Review der ganzen Publikation

Open Access-Status

Hybrid

Lizenz

Zitation

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

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