2004
DOI: 10.1021/jp040231i
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Changes in Microemulsion and Protein Structure in IgG−AOT−Brine−Isooctane Systems

Abstract: Changes in structure of protein molecules and water-in-oil (w/o) microemulsion aggregates were investigated using the large protein immunoglobulin G (IgG, MW 155,000) and an equivolume oil/water mixture composed of brine, sulfosuccinic acid bis [2-ethylhexyl]ester (sodium salt) (AOT), and isooctane. The protein solution in the microemulsion phase was metastable: over time this solution changed, as protein and w/o droplets aggregated and precipitated to the interface between aqueous and organic phases. Such fac… Show more

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Cited by 11 publications
(6 citation statements)
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“…A similar size dependency of w/o microemulsion droplets on the AOT concentration was observed previously using photon correlation spectroscopy . At higher AOT concentrations, the radius (and the molar ratio of water-to-surfactant) becomes constant, as expected; , in this region, larger amounts of water in the organic phase are accommodated within an increased number of droplets, whose size remains the same. For the sample with 0.2 M AOT, the SAXS curve could not be fit with a structure factor of hard-sphere interactions alone, and the Yukawa tail structure factor (5) was used to fit the data, with parameters A = 4 k B T and k = 0.27.…”
Section: Resultssupporting
confidence: 84%
See 1 more Smart Citation
“…A similar size dependency of w/o microemulsion droplets on the AOT concentration was observed previously using photon correlation spectroscopy . At higher AOT concentrations, the radius (and the molar ratio of water-to-surfactant) becomes constant, as expected; , in this region, larger amounts of water in the organic phase are accommodated within an increased number of droplets, whose size remains the same. For the sample with 0.2 M AOT, the SAXS curve could not be fit with a structure factor of hard-sphere interactions alone, and the Yukawa tail structure factor (5) was used to fit the data, with parameters A = 4 k B T and k = 0.27.…”
Section: Resultssupporting
confidence: 84%
“…[9][10][11][12][13][14] We have become interested in a somewhat different phenomenon: the effect of protein on surfactant self-assembly in two-phase systems consisting of both oil and water. [15][16][17][18][19][20] Selfassembly is more unconstrained in such two-phase mixtures, and more far-reaching changes in phase morphology can potentially be observed. Water-in-oil microemulsion droplets can change their size by taking up or releasing water from the coexisting aqueous phase, while oil-in-water droplets can do the same with the adjacent oil phase.…”
Section: Introductionmentioning
confidence: 99%
“…Previous research in single-phase organic , or aqueous surfactant solutions, as well as in aqueous/organic mixtures, provides evidence that proteins can shift the phase boundaries of such solutions. These effects of proteins on surfactant phase behavior are generally associated with intimate interactioneither peripheral or intrinsicbetween the protein molecule and surfactant, often accompanied by changes in nanostructure morphology.…”
Section: Introductionmentioning
confidence: 99%
“…In water and oil mixtures, amphiphilic molecules form monolayer membranes at the oil -water interface, known as microemulsion droplets. Among the various structures formed by amphiphilic molecules, vesicles and microemulsion droplets have closed membrane surfaces formed by the amphiphilic molecules and have important functions as nanometre-and micrometre-sized membrane capsules in biological systems [1,2] and molecular carrier systems. [3,4] When guest molecules are confined in the capsules, their translational motions are restricted and the interaction between the guest molecule and the membrane is enhanced.…”
Section: Introductionmentioning
confidence: 99%