Design of surfactants suitable for protein extraction by reversed micelles

Goto, Masahiro; Ono, Tsutomu; Nakashio, Fumiyuki; Hatton, T. Alan

doi:10.1002/(sici)1097-0290(19970405)54:1<26::aid-bit3>3.0.co;2-#

Cited by 62 publications

(29 citation statements)

References 27 publications

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“…Reverse micelles are thermodynamically stable assemblies of surfactant molecules organized around a water core and will form spontaneously as transparent solutions in a low polarity liquid. Reverse micelles have been considered for a range of applications, including molecular separations and reaction processes (20)(21)(22)(23)(24). Recently, perfluoropolyether microemulsions have been studied as potential hosts for various chemical reactions in solvents with low environmental impact such as supercritical carbon dioxide (25).…”

Section: Resultsmentioning

confidence: 99%

“…Stable reverse micelles of AOT large enough to accommodate aqueous solutions of proteins of significant size have been demonstrated to form in a variety of liquid alkanes (26)(27)(28)(29). Dozens of proteins, many exceeding 50 kDa in size, have been successfully solubilized by reverse micelles in organic solvents (20)(21)(22)(23)(24)(25).…”

Section: Resultsmentioning

confidence: 99%

“…Even greater benefits are anticipated by using critical ethane, though significantly higher pressures will be required, perhaps up to 200 bar (34). Nevertheless, given the long history of encapsulating proteins of significant size in reverse micelle systems (20)(21)(22)(23)(24), this approach holds the promise of extending NMR-based structural analysis to soluble proteins of 50 kDa and beyond. The approach is also applicable to other biopolymers such as nucleic acids, carbohydrates, and, perhaps most important, membrane proteins.…”

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confidence: 99%

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High-resolution NMR of encapsulated proteins dissolved in low-viscosity fluids

Wand

Ehrhardt

Flynn

1998

Proc. Natl. Acad. Sci. U.S.A.

123

167

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The majority of known proteins are too large to be comprehensively examined by solution NMR methods, primarily because they tumble too slowly in solution. Here we introduce an approach to making the NMR relaxation properties of large proteins amenable to modern solution NMR techniques. The encapsulation of a protein in a reverse micelle dissolved in a low-viscosity fluid allows it to tumble as fast as a much smaller protein. The approach is demonstrated and validated with the protein ubiquitin encapsulated in reverse micelles prepared in a variety of alkane solvents.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

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High-resolution NMR of encapsulated proteins dissolved in low-viscosity fluids

Wand

Ehrhardt

Flynn

1998

Proc. Natl. Acad. Sci. U.S.A.

123

167

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“…To understand the extraction mechanism, many efforts have been made to study the effects of various experimental conditions, which include the natures and concentrations of proteins, surfactants, and aqueous electrolytes and the pH of the aqueous phase. [2][3][4][5][6][11][12][13][14][15][16][17][18][19][20][21] It is generally recognized that the electrostatic interactions between a protein and surfactants play an important role in the formation of reverse micelles containing proteins. It has also been claimed that the electrostatic interactions of a protein with a bulk oil/water (O/W) interface play the dominant role in the inclusion of a protein in a reverse micelle at the O/W interface.…”

Section: Introductionmentioning

confidence: 99%

Electrochemical Aspects of the Reverse Micelle Extraction of Proteins

Osakai

Shinohara

2008

ANAL. SCI.

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The mechanism of the solvent extraction of cytochrome c (Cyt c) via reverse micelle formation was studied from an electrochemical point of view. Potentiometric measurements showed that the Galvani potential difference of the oil/water (O/W) interface played a crucial role in the spontaneous extraction of Cyt c with bis(2-ethylhexyl)sulfosuccinate (AOT). However, the dependence of the extraction efficiency on the concentration of an aqueous electrolyte (KCl) could be explained not by the effect of the interfacial potential, but by the change in the interfacial tension (g). Electrocapillary measurements showed that the adsorption of AOT anions to the O/W interface resulted in a significant decrease of g in a higher potential range, where reverse micelles were formed. The bottom level of g in the higher potential range was increased with [KCl]. The lower extraction efficiency for higher [KCl]'s was elucidated by a "size exclusion effect". This was also supported by water-content measurements by the Karl Fisher method.

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“…Membrane fusion, 41 reversed micellar extaction, 42 formation of AOT microemulsions at an oil/water interfrace, 43 formation and accumulation of lipid nanotubes, 44 chemical oscillation phenomena, [45][46][47][48] unusual current generation triggered by fusion of emulsion, 49 and hybridization of complementary single-stranded DNA, 50 are examples of them. We believe the experimental technique shown here will provide a new and useful tool to investigate phenomena where dynamic behaviors of molecular assemblies play important roles.…”

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confidence: 99%