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231224s2015 xx |||||o 00| ||eng c |
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|a 10.1021/la504606x
|2 doi
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|a pubmed24n0818.xml
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|a (DE-627)NLM245481435
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|a (NLM)25603188
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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|a Hayes, Douglas G
|e verfasserin
|4 aut
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|a Effect of protein incorporation on the nanostructure of the bicontinuous microemulsion phase of Winsor-III systems
|b a small-angle neutron scattering study
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|c 2015
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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|a Date Completed 26.10.2015
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|a Date Revised 17.02.2015
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|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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|a Journal Article
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|a Research Support, U.S. Gov't, Non-P.H.S.
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|a Aerosols
|2 NLM
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|a Emulsions
|2 NLM
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|a Heptanes
|2 NLM
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|a Oils
|2 NLM
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|a Proteins
|2 NLM
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|a Water
|2 NLM
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|a 059QF0KO0R
|2 NLM
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|a Gomez del Rio, Javier A
|e verfasserin
|4 aut
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|a Ye, Ran
|e verfasserin
|4 aut
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|a Urban, Volker S
|e verfasserin
|4 aut
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|a Pingali, Sai Venkatesh
|e verfasserin
|4 aut
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|a O'Neill, Hugh M
|e verfasserin
|4 aut
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|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1992
|g 31(2015), 6 vom: 17. Feb., Seite 1901-10
|w (DE-627)NLM098181009
|x 1520-5827
|7 nnns
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|g volume:31
|g year:2015
|g number:6
|g day:17
|g month:02
|g pages:1901-10
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|u http://dx.doi.org/10.1021/la504606x
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