Electrochemistry at the interface between two immiscible electrolyte solutions (IUPAC Technical Report)

Samec, Zdeněk

doi:10.1351/pac200476122147

Cited by 334 publications

(344 citation statements)

References 100 publications

(172 reference statements)

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“…In this report, the electroactivity of myoglobin (Mb) at the interface between two immiscible electrolyte solutions (ITIES) [1] is presented. Mb is a globular protein containing a haem group, comprised of a single chain of 153 amino acids with a molecular mass of 16.7 kDa and an iso-electric point of ~7.3 [2].…”

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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“…Electrochemical methods provide important analytical tools for protein detection [1]. 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].…”

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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“…1. As in conventional solid electrode|solution electrochemistry, the current can arise from electron transfer across ITIES and additionally it can also arise from the transfer of ions across ITIES [13][14][15][16][17]. This renders the ITIES ideally suited to the study of ion partitioning across two immiscible phases, which combined with traditional techniques allows for the contribution of ions and neutral compounds to be determined, as shown in the studies of Bouchard et al [18,19], Reymond et al [11], and Nagatani et al [20].…”

Section: Determination Of Partition Coefficientsmentioning

confidence: 99%

“…This is demonstrated by Eq. (2), where P i and P i 0 are the partition coefficient and standard partition coefficient, respectively, of ion i, Δφ is the Galvani potential, tr,i , o is the standard Gibbs energy of transfer for ion i from the aqueous phase to the organic phase, z i is the charge of ion i, F is the Faraday constant, R is the universal gas constant and T is the temperature [14,15].…”

Section: Determination Of Partition Coefficientsmentioning

confidence: 99%

Use of voltammetry for in vitro equilibrium and transport studies of ionisable drugs

et al. 2014

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In this review, we will briefly outline the voltammetric investigations of the transfer of ionisable drugs at the interface between two immiscible electrolyte solutions. The voltammetric techniques enable the determination of some key in vitro properties of ionisable drugs, including partition coefficient, diffusioncoefficient and membrane permeability. Some successful applications will be highlighted, together with the background methodologies.

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Electrochemistry at the interface between two immiscible electrolyte solutions (IUPAC Technical Report)

Cited by 334 publications

References 100 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

Electrochemical behaviour of denatured haemoglobin at the liquid|liquid interface

Use of voltammetry for in vitro equilibrium and transport studies of ionisable drugs

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