Effect of Protein Incorporation on the Nanostructure of the Bicontinuous Microemulsion Phase of Winsor-III Systems: A Small-Angle Neutron Scattering Study
journal contributionposted on 17.02.2015, 00:00 by Douglas G. Hayes, Javier A. Gomez del Rio, Ran Ye, Volker S. Urban, Sai Venkatesh Pingali, Hugh M. O’Neill
Small-angle neutron scattering (SANS) analysis using the Teubner–Strey model has been employed to evaluate the effect of protein incorporation into the middle, bicontinuous microemulsion (BμE) phase of Winsor-III (WIII) systems formed by an aerosol-OT (AOT)/alkyl ethoxylate mixed surfactant system to understand better the extraction of proteins into and out of BμEs and to study the effect of proteins on a system that serves as a biomimetic analog of cell membranes. Under conditions of high salinity, the incorporation of positively charged proteins cytochrome c, lysozyme, and α-chymotrypsin, near their solubilization limit in the BμEs promoted the release of water and oil from the BμEs, a decrease in the quasi-periodic repeat distance (d), an increase in ordering (a decrease in the amphiphilicity factor, fa) for the surfactant monolayers, and a decrease in the surface area per surfactant headgroup, suggesting that the proteins affected the self-assembly of components in the BμE phase and produced Debye shielding of AOT’s sulfonate headgroup. For WIII systems possessing lower salinity, cytochrome c reduced the efficiency of surfactant in the BμE phase, noted by increases in d and fa, suggesting that the enzyme and AOT underwent ion pairing. The results of this study demonstrate the importance of ionic strength to modulate protein–surfactant interactions, which in turn will control the release of proteins encapsulated in the BμEs, relevant to WIII-based protein extraction and controlled release from BμE delivery systems, and demonstrate the utility of BμEs as a model system to understand the effect of proteins on biomembranes.