The value and promise of micelle encapsulation of proteins has been demonstrated in experimental studies of protein structure, dynamics, and function. Currently, however, there is an incomplete understanding of the micelle environment and its influence on the structure and dynamics of proteins encapsulated in normal and reverse micelles. In recent years, reverse micelle systems have been developed for the study of structural and functional properties of soluble proteins. Pioneering work has explored the use of a variety of surfactants, including anionic, cationic, and zwitterionic surfactants and mixtures. This approach has led to good results for a variety of protein systems. In spite of these successes, the actual state and environment of the encapsulated protein must be indirectly determined. Experimental analysis often assumes a spherical reverse micelle environment with minimal interaction between the encapsulated protein and the surfactant boundary. However, simulation studies have suggested that there can be substantial interaction between the encapsulated protein and the surfactant layer, the degree of interaction being highly sequence and surfactant specific. At this time there exists no theoretical understanding of how surfactant composition influences the structure and dynamics of reverse micelles, the critical micelle concentration, the distribution of micelle size, or the interaction between the water-surfactant interface and the solubilized peptide or protein. Recent efforts to develop a first principles approach to the theoretical characterization of reverse micelles with and without encapsulated protein will be discussed.

Complex role of solvation in micelle and reverse micelle environments

251st National Meeting (2016)

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