Ionic liquids (ILs) have potential applications as selective protein stabilization agents in the biotechnology industry. It is known that ILs as solution additives could stabilize desired proteins and destabilize unwanted proteins, or destabilize proteins to promote unfolding and materials self-assembly. However, the exact underlying mechanism by which they increase the overall stability of the protein is not yet known. We have used a combination of enzymatic assays, fluorescence spectroscopy, and circular dichroism spectroscopy to understand the interactions of several IL systems with the copper-binding proteins Azurin (Pseudomonas aeruginosa) and laccase (Trametes Versicolor). Specifically, we initially focused on how the different ionic liquids affected the stability of the proteins in structural denaturation assays. These studies will provide new insight into the molecular ion-protein interactions responsible for protein stabilization and destabilization by ILs and enable the design of biomaterials for selective protein engineering or to improve therapies focused on specific protein targets.

Effect of ionic liquids on copper protein stability

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.