Within the cell, proteins are surrounded by other large molecules that may cause extreme crowding, which may result in three-dimensional confinement. The effects of confinement on protein stability are yet to be understood well. Many protein stability studies have been performed in bulk aqueous solution. In this study, reverse micelles were used to encapsulate the protein to create a confined environment similar to that of a cell. Reverse micelles are spontaneously-organizing mixtures composed of an aqueous core that is surrounded by an organic layer that is stabilized using surfactants. This allows us to investigate quinary interactions of proteins and their stabilizing and destabilizing effects. The reverse micelles were created using cetyltriammonium bromide (CTAB), decylmonacyl glycerol (10MAG) and lauryldimethylammonium-N-oxide (LDAO). Chemically induced unfolding studies of hen egg white lysozyme (HEWL) and red fluorescent protein (RFP) were performed using guanidine and urea. Structural studies of the proteins were performed using fluorescence spectroscopy. A spectral shift indicates protein unfolding and was observed in bulk and confined environments. The midpoint of the unfolding transition shifts in the reverse micelle, thereby revealing the thermodynamic impact of confinement on protein stability.

Determining confinement effects on protein stability using reverse micelle encapsulation of model proteins

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.