Secondary Structural Changes in Proteins as a Result of Electroadsorption at Aqueous-Organogel Interfaces
The electroadsorption of proteins at aqueous-organic interfaces offers the possibility to examine protein structural rearrangements upon interaction with lipophilic phases, without modifying the bulk protein or relying on a solid support. The aqueous-organic interface has already provided a simple m...
| Main Authors: | , , , , , , , , |
|---|---|
| Format: | Journal Article |
| Language: | English |
| Published: |
AMER CHEMICAL SOC
2019
|
| Subjects: | |
| Online Access: | http://hdl.handle.net/20.500.11937/79098 |
| _version_ | 1848764000130564096 |
|---|---|
| author | Booth, S.G. Felisilda, Bren Alvarez De Eulate, E. Gustafsson, O.J.R. Arooj, Mahreen Mancera, Ricardo Dryfe, R.A.W. Hackett, Mark Booth, S.G. Arrigan, Damien |
| author_facet | Booth, S.G. Felisilda, Bren Alvarez De Eulate, E. Gustafsson, O.J.R. Arooj, Mahreen Mancera, Ricardo Dryfe, R.A.W. Hackett, Mark Booth, S.G. Arrigan, Damien |
| author_sort | Booth, S.G. |
| building | Curtin Institutional Repository |
| collection | Online Access |
| description | The electroadsorption of proteins at aqueous-organic interfaces offers the possibility to examine protein structural rearrangements upon interaction with lipophilic phases, without modifying the bulk protein or relying on a solid support. The aqueous-organic interface has already provided a simple means of electrochemical protein detection, often involving adsorption and ion complexation; however, little is yet known about the protein structure at these electrified interfaces. This work focuses on the interaction between proteins and an electrified aqueous-organic interface via controlled protein electroadsorption. Four proteins known to be electroactive at such interfaces were studied: lysozyme, myoglobin, cytochrome c, and hemoglobin. Following controlled protein electroadsorption onto the interface, ex situ structural characterization of the proteins by FTIR spectroscopy was undertaken, focusing on secondary structural traits within the amide I band. The structural variations observed included unfolding to form aggregated antiparallel β-sheets, where the rearrangement was specifically dependent on the interaction with the organic phase. This was supported by MALDI ToF MS measurements, which showed the formation of protein-anion complexes for three of these proteins, and molecular dynamic simulations, which modeled the structure of lysozyme at an aqueous-organic interface. On the basis of these findings, the modulation of protein secondary structure by interfacial electrochemistry opens up unique prospects to selectively modify proteins. © |
| first_indexed | 2025-11-14T11:12:23Z |
| format | Journal Article |
| id | curtin-20.500.11937-79098 |
| institution | Curtin University Malaysia |
| institution_category | Local University |
| language | English |
| last_indexed | 2025-11-14T11:12:23Z |
| publishDate | 2019 |
| publisher | AMER CHEMICAL SOC |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | curtin-20.500.11937-790982021-03-05T02:31:01Z Secondary Structural Changes in Proteins as a Result of Electroadsorption at Aqueous-Organogel Interfaces Booth, S.G. Felisilda, Bren Alvarez De Eulate, E. Gustafsson, O.J.R. Arooj, Mahreen Mancera, Ricardo Dryfe, R.A.W. Hackett, Mark Booth, S.G. Arrigan, Damien Science & Technology Physical Sciences Technology Chemistry, Multidisciplinary Chemistry, Physical Materials Science, Multidisciplinary Chemistry Materials Science EGG-WHITE LYSOZYME ELECTROCHEMICAL-BEHAVIOR INFRARED-SPECTROSCOPY CIRCULAR-DICHROISM LIQUID HEMOGLOBIN IONS AGGREGATION VOLTAMMETRY ADSORPTION The electroadsorption of proteins at aqueous-organic interfaces offers the possibility to examine protein structural rearrangements upon interaction with lipophilic phases, without modifying the bulk protein or relying on a solid support. The aqueous-organic interface has already provided a simple means of electrochemical protein detection, often involving adsorption and ion complexation; however, little is yet known about the protein structure at these electrified interfaces. This work focuses on the interaction between proteins and an electrified aqueous-organic interface via controlled protein electroadsorption. Four proteins known to be electroactive at such interfaces were studied: lysozyme, myoglobin, cytochrome c, and hemoglobin. Following controlled protein electroadsorption onto the interface, ex situ structural characterization of the proteins by FTIR spectroscopy was undertaken, focusing on secondary structural traits within the amide I band. The structural variations observed included unfolding to form aggregated antiparallel β-sheets, where the rearrangement was specifically dependent on the interaction with the organic phase. This was supported by MALDI ToF MS measurements, which showed the formation of protein-anion complexes for three of these proteins, and molecular dynamic simulations, which modeled the structure of lysozyme at an aqueous-organic interface. On the basis of these findings, the modulation of protein secondary structure by interfacial electrochemistry opens up unique prospects to selectively modify proteins. © 2019 Journal Article http://hdl.handle.net/20.500.11937/79098 10.1021/acs.langmuir.8b04227 English AMER CHEMICAL SOC restricted |
| spellingShingle | Science & Technology Physical Sciences Technology Chemistry, Multidisciplinary Chemistry, Physical Materials Science, Multidisciplinary Chemistry Materials Science EGG-WHITE LYSOZYME ELECTROCHEMICAL-BEHAVIOR INFRARED-SPECTROSCOPY CIRCULAR-DICHROISM LIQUID HEMOGLOBIN IONS AGGREGATION VOLTAMMETRY ADSORPTION Booth, S.G. Felisilda, Bren Alvarez De Eulate, E. Gustafsson, O.J.R. Arooj, Mahreen Mancera, Ricardo Dryfe, R.A.W. Hackett, Mark Booth, S.G. Arrigan, Damien Secondary Structural Changes in Proteins as a Result of Electroadsorption at Aqueous-Organogel Interfaces |
| title | Secondary Structural Changes in Proteins as a Result of Electroadsorption at Aqueous-Organogel Interfaces |
| title_full | Secondary Structural Changes in Proteins as a Result of Electroadsorption at Aqueous-Organogel Interfaces |
| title_fullStr | Secondary Structural Changes in Proteins as a Result of Electroadsorption at Aqueous-Organogel Interfaces |
| title_full_unstemmed | Secondary Structural Changes in Proteins as a Result of Electroadsorption at Aqueous-Organogel Interfaces |
| title_short | Secondary Structural Changes in Proteins as a Result of Electroadsorption at Aqueous-Organogel Interfaces |
| title_sort | secondary structural changes in proteins as a result of electroadsorption at aqueous-organogel interfaces |
| topic | Science & Technology Physical Sciences Technology Chemistry, Multidisciplinary Chemistry, Physical Materials Science, Multidisciplinary Chemistry Materials Science EGG-WHITE LYSOZYME ELECTROCHEMICAL-BEHAVIOR INFRARED-SPECTROSCOPY CIRCULAR-DICHROISM LIQUID HEMOGLOBIN IONS AGGREGATION VOLTAMMETRY ADSORPTION |
| url | http://hdl.handle.net/20.500.11937/79098 |