Effect of protein incorporation on the nanostructure of the bicontinuous microemulsion phase of Winsor-III systems : a small-angle neutron scattering study

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 t...

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Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1992. - 31(2015), 6 vom: 17. Feb., Seite 1901-10
1. Verfasser: Hayes, Douglas G (VerfasserIn)
Weitere Verfasser: Gomez del Rio, Javier A, Ye, Ran, Urban, Volker S, Pingali, Sai Venkatesh, O'Neill, Hugh M
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2015
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, U.S. Gov't, Non-P.H.S. Aerosols Emulsions Heptanes Oils Proteins Water 059QF0KO0R
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520 |a 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 
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700 1 |a Gomez del Rio, Javier A  |e verfasserin  |4 aut 
700 1 |a Ye, Ran  |e verfasserin  |4 aut 
700 1 |a Urban, Volker S  |e verfasserin  |4 aut 
700 1 |a Pingali, Sai Venkatesh  |e verfasserin  |4 aut 
700 1 |a O'Neill, Hugh M  |e verfasserin  |4 aut 
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