Electrochemical Extraction of Proteins by Reverse Micelle Formation

Shinshi, Mariko; Sugihara, Takayasu; Osakai, Toshiyuki; Goto, Masahiro

doi:10.1021/la060858n

Cited by 71 publications

(97 citation statements)

References 70 publications

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“…Osakai et al used surfactants in the organic phase as the basis for protein detection and found that cytochrome c could be transferred across the ITIES [33][34][35]. A range of proteins have been studied at the ITIES in the absence of surfactants and it was found that the proteins did not transfer across the ITIES but adsorbed there and facilitated the transfer of the organic anion to the aqueous phase [24,[26][27][28].…”

Section: Introductionmentioning

confidence: 99%

Electrochemical behaviour of myoglobin at an array of microscopic liquid–liquid interfaces

O'Sullivan

Arrigan

2012

Electrochimica Acta

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Electrochemistry at liquid-liquid interfaces, or at interfaces between two immiscible electrolyte solutions (ITIES), provides a basis for the non-redox detection of biological molecules, based on iontransfer or adsorption processes. The electroactivity of myoglobin at an array of micron-sized liquidorganogel interfaces was investigated. The µITIES array was patterned with a silicon membrane consisting of an array of eight pores with radii of ~12.8 µm and a pore to pore separation of ~400 µm.Using cyclic voltammetry at the ITIES, the protein was shown to adsorb at the interface and facilitate the transfer of the organic phase electrolyte anions to the aqueous side of the interface. The electrochemical current response was linear with concentration in the range of 1 -6 µM, with corresponding surface coverage of 10 -50 pmol cm -2 . The reverse peak currents was found to be proportional to the voltammetric scan rate, indicating a desorption process. The detection of the protein was only possibly when the pH of the aqueous phase solution was below the pI of the protein. The steady-state simple ion transfer behaviour of tetraethylammonium cation was decreased on the forward sweep, providing a qualitative indication of the presence of adsorbed protein at the interface.Increasing the ionic strength of the aqueous phase resulted in enhanced peak currents, possibly due to aggregation of protein precipitates in the aqueous solution. UV/Vis absorbance spectroscopy was used 1 ISE Member.2 | P a g e to investigate the effects of various aqueous electrolyte solutions on the structure of the protein, and it was shown that at low pH the protein is at least partially denatured. These results provide the basis for label-free detection of myoglobin at the ITIES.

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Section: Introductionmentioning

confidence: 99%

Electrochemical behaviour of myoglobin at an array of microscopic liquid–liquid interfaces

O'Sullivan

Arrigan

2012

Electrochimica Acta

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“…The electrochemical behaviour of proteins [9][10][11][12][13][14][15] at the interface between two immiscible electrolyte solutions (ITIES) has been reported recently. Proteins adsorb at the interface and assist the transfer of anions from the organic phase electrolyte to the aqueous phase.…”

Section: Introductionmentioning

confidence: 99%

Haemoglobin unfolding studies at the liquid–liquid interface

Herzog

Nolan

Arrigan

2011

Electrochemistry Communications

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Abstract:The electrochemical behaviour of haemoglobin denatured using different concentrations of urea was investigated at the liquid|liquid interface. The reverse peak current varied with the concentration of urea, allowing the building of the unfolding curve, which compares well with UV-Vis absorbance results. Thermodynamic parameters, such as the change in free energy of folding in water, w G ∆ , and the index of the compactness of the protein, m, were extracted from the experimental data. The work here presents a simple electrochemical method for the study of protein unfolding by electrochemistry at the liquid | liquid interface.

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“…Amongst these, electrochemistry at polarised liquid|liquid interfaces has been used for the investigation of non-redox electrochemistry [2,3] and electroanalytical determination [4] of a range of ions. Recently, a variety of large polycationic molecules have been studied at the liquid|liquid interface, EC09-2006, revised 16Dec2009 2 including dendrimers [5], peptides [6] and proteins [7][8][9][10][11][12][13][14][15][16][17][18][19][20]. We have recently investigated the electrochemical behaviour of haemoglobin [15][16][17], insulin [18] and lysozyme [19] at the liquid | liquid interface.…”

Section: Introductionmentioning

confidence: 99%

Electrochemical behaviour of denatured haemoglobin at the liquid|liquid interface

Herzog¹,

Eichelmann-Daly²,

Arrigan³

2010

Electrochemistry Communications

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Abstract:We report here the influence of chemical denaturation of haemoglobin on its electrochemical behaviour at the polarised liquid|liquid interface. Denaturation with urea resulted in a modification of the haemoglobin electrochemical behaviour, with the disappearance of the forward transfer peak and a decrease of the reverse peak current. Although the reverse peak current increased linearly with the concentration of denatured haemoglobin in the aqueous phase, the slope of the current-concentration plot was three times lower than that for native haemoglobin over the 0.1 -1 M concentration range. These results indicate the sensitivity of electrochemistry at liquid|liquid interfaces to protein tertiary structure.

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Electrochemical Extraction of Proteins by Reverse Micelle Formation

Cited by 71 publications

References 70 publications

Electrochemical behaviour of myoglobin at an array of microscopic liquid–liquid interfaces

Electrochemical behaviour of myoglobin at an array of microscopic liquid–liquid interfaces

Haemoglobin unfolding studies at the liquid–liquid interface

Electrochemical behaviour of denatured haemoglobin at the liquid|liquid interface

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