Within the cell, proteins are subject to a crowded environment which has a thermodynamic impact on their stability. Most protein stability studies have been performed in bulk solution where environmental influences are negligible. By encapsulating proteins in reverse micelles, we are able to model the most extreme crowded condition found within the cell, i.e. confinement. Reverse micelles are spontaneously-organizing mixtures composed of an aqueous core surrounded by an organic layer stabilized by surfactants. Under optimized conditions, proteins can be encapsulated in reverse micelles while maintaining their native structure. Reverse micelle encapsulation also allows us to investigate quinary interactions and their stabilizing or destabilizing effect on globular proteins by altering the charge distribution of the surfactant interface. Chemical denaturation studies using guanidine and urea in both an aqueous and confined environment were performed using bovine serum albumin (BSA) as a model protein. Reverse micelles were manufactured using cetyltrimethylammonium (CTAB) and hexanol as well as decylmonacyl glycerol (10MAG) and lauryldimethylammonium-N-oxide (LDAO). Unfolding was measured by monitoring intrinsic protein fluorescence with a spectral shift confirming denaturation. Thermodynamic analyses revealed a shift in the midpoint of the unfolding transition in confined studies indicating an impact on protein stability. By titrating cationic and anionic surfactants into our reverse micelles, we can quantify charge dependent quinary interactions.

Dissecting confinement effects on stability using reverse micelle encapsulation of bovine serum albumin

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.