Exploiting cyclodextrins as artificial chaperones to enhance enzyme protection through supramolecular engineering
Source abstract
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.
Source: europepmc · Quality: candidate unverified · Source record ↗
Research context
OpenAlex topics: Protein Structure and Dynamics · Enzyme Structure and Function · Protein purification and stability
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
School of Life Science, University of Applied Sciences and Arts Northwestern Switzerland, Hofackerstrasse 30, Muttenz CH-4132, Switzerland
Department of Biology, Faculty of Sciences, University of Guilan, Rasht, Iran
Swiss Nanoscience Institute, Klingelbergstrasse 82, Basel CH-4056, Switzerland
Barcelona Supercomputing Center (BSC), 08034 Barcelona, Spain
Faculty of Pharmacy and Food Science, Universitat de Barcelona (UB), 08007 Barcelona, Spain
Instituto de Catalisis y Petroleoquimica (ICP), CSIC, 28049 Madrid, Spain
Institution for Research and Advanced Studies (ICREA), 08010 Barcelona, Spain
Funding
H2020 Societal Challenges · Ministerio de Ciencia e Innovación · Agencia Estatal de Investigación · European Regional Development Fund
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