Impact of a surfactant on the electroactivity of proteins at an aqueous-organogel microinterface array
The impact of surfactant addition to the organic phase on the electroactivity of proteins at the aqueous-organogel interface was examined by voltammetry. The presence of bis(2-ethylhexyl)sulfosuccinate (AOT) in the organogel phase, as the sodium salt, caused marked changes in the peak currents for m...
| Main Authors: | , |
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| Format: | Journal Article |
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American Chemical Society
2013
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| Online Access: | http://hdl.handle.net/20.500.11937/15801 |
| _version_ | 1848748992149585920 |
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| author | O'Sullivan, S. Arrigan, Damien |
| author_facet | O'Sullivan, S. Arrigan, Damien |
| author_sort | O'Sullivan, S. |
| building | Curtin Institutional Repository |
| collection | Online Access |
| description | The impact of surfactant addition to the organic phase on the electroactivity of proteins at the aqueous-organogel interface was examined by voltammetry. The presence of bis(2-ethylhexyl)sulfosuccinate (AOT) in the organogel phase, as the sodium salt, caused marked changes in the peak currents for myoglobin detection. The protein desorption voltammetric peak exhibited a 6-fold increase in the current compared to the corresponding experiment without surfactant. Interfacial coverage showed a 17-fold increase in the adsorbed protein at the interface, from 50 pmol cm-2, in the absence of surfactant, to 850 pmol cm-2, in the presence of 10 mM surfactant. Additionally, the presence of the surfactant resulted in a second pair of adsorption/desorption peaks at lower potentials and in a change in the capacitance of the system. The formation of surfactant-protein and surfactant-protein-organic anion deposits is proposed on the basis of these features, leading to increased voltammetric signals for myoglobin, hemoglobin, and cytochrome c. The mechanism of protein-surfactant interaction was probed by using the surfactant as the anion in the organic phase electrolyte salt. Repetitive cyclic voltammetry of cytochrome c showed that in the presence of surfactant there was an enhancement of the signal, caused by a build-up of the protein-surfactant-electrolyte anion assembly at the interface. These findings provide the basis for surfactant-modified interfaces to enhance the electroanalytical performance for protein detection. |
| first_indexed | 2025-11-14T07:13:51Z |
| format | Journal Article |
| id | curtin-20.500.11937-15801 |
| institution | Curtin University Malaysia |
| institution_category | Local University |
| last_indexed | 2025-11-14T07:13:51Z |
| publishDate | 2013 |
| publisher | American Chemical Society |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | curtin-20.500.11937-158012017-09-13T16:09:10Z Impact of a surfactant on the electroactivity of proteins at an aqueous-organogel microinterface array O'Sullivan, S. Arrigan, Damien The impact of surfactant addition to the organic phase on the electroactivity of proteins at the aqueous-organogel interface was examined by voltammetry. The presence of bis(2-ethylhexyl)sulfosuccinate (AOT) in the organogel phase, as the sodium salt, caused marked changes in the peak currents for myoglobin detection. The protein desorption voltammetric peak exhibited a 6-fold increase in the current compared to the corresponding experiment without surfactant. Interfacial coverage showed a 17-fold increase in the adsorbed protein at the interface, from 50 pmol cm-2, in the absence of surfactant, to 850 pmol cm-2, in the presence of 10 mM surfactant. Additionally, the presence of the surfactant resulted in a second pair of adsorption/desorption peaks at lower potentials and in a change in the capacitance of the system. The formation of surfactant-protein and surfactant-protein-organic anion deposits is proposed on the basis of these features, leading to increased voltammetric signals for myoglobin, hemoglobin, and cytochrome c. The mechanism of protein-surfactant interaction was probed by using the surfactant as the anion in the organic phase electrolyte salt. Repetitive cyclic voltammetry of cytochrome c showed that in the presence of surfactant there was an enhancement of the signal, caused by a build-up of the protein-surfactant-electrolyte anion assembly at the interface. These findings provide the basis for surfactant-modified interfaces to enhance the electroanalytical performance for protein detection. 2013 Journal Article http://hdl.handle.net/20.500.11937/15801 10.1021/ac302222u American Chemical Society restricted |
| spellingShingle | O'Sullivan, S. Arrigan, Damien Impact of a surfactant on the electroactivity of proteins at an aqueous-organogel microinterface array |
| title | Impact of a surfactant on the electroactivity of proteins at an aqueous-organogel microinterface array |
| title_full | Impact of a surfactant on the electroactivity of proteins at an aqueous-organogel microinterface array |
| title_fullStr | Impact of a surfactant on the electroactivity of proteins at an aqueous-organogel microinterface array |
| title_full_unstemmed | Impact of a surfactant on the electroactivity of proteins at an aqueous-organogel microinterface array |
| title_short | Impact of a surfactant on the electroactivity of proteins at an aqueous-organogel microinterface array |
| title_sort | impact of a surfactant on the electroactivity of proteins at an aqueous-organogel microinterface array |
| url | http://hdl.handle.net/20.500.11937/15801 |