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dc.contributor.authorBooth, S.G.
dc.contributor.authorFelisilda, Bren
dc.contributor.authorAlvarez De Eulate, E.
dc.contributor.authorGustafsson, O.J.R.
dc.contributor.authorArooj, Mahreen
dc.contributor.authorMancera, Ricardo
dc.contributor.authorDryfe, R.A.W.
dc.contributor.authorHackett, Mark
dc.contributor.authorBooth, S.G.
dc.contributor.authorArrigan, Damien
dc.date.accessioned2020-05-14T03:16:23Z
dc.date.available2020-05-14T03:16:23Z
dc.date.issued2019
dc.identifier.citationBooth, S.G. and Felisilda, B.M.B. and Alvarez De Eulate, E. and Gustafsson, O.J.R. and Arooj, M. and Mancera, R.L. and Dryfe, R.A.W. et al. 2019. Secondary Structural Changes in Proteins as a Result of Electroadsorption at Aqueous-Organogel Interfaces. Langmuir. 35 (17): pp. 5821-5829.
dc.identifier.urihttp://hdl.handle.net/20.500.11937/79098
dc.identifier.doi10.1021/acs.langmuir.8b04227
dc.description.abstract

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. ©

dc.languageEnglish
dc.publisherAMER CHEMICAL SOC
dc.subjectScience & Technology
dc.subjectPhysical Sciences
dc.subjectTechnology
dc.subjectChemistry, Multidisciplinary
dc.subjectChemistry, Physical
dc.subjectMaterials Science, Multidisciplinary
dc.subjectChemistry
dc.subjectMaterials Science
dc.subjectEGG-WHITE LYSOZYME
dc.subjectELECTROCHEMICAL-BEHAVIOR
dc.subjectINFRARED-SPECTROSCOPY
dc.subjectCIRCULAR-DICHROISM
dc.subjectLIQUID
dc.subjectHEMOGLOBIN
dc.subjectIONS
dc.subjectAGGREGATION
dc.subjectVOLTAMMETRY
dc.subjectADSORPTION
dc.titleSecondary Structural Changes in Proteins as a Result of Electroadsorption at Aqueous-Organogel Interfaces
dc.typeJournal Article
dcterms.source.volume35
dcterms.source.number17
dcterms.source.startPage5821
dcterms.source.endPage5829
dcterms.source.issn0743-7463
dcterms.source.titleLangmuir
dc.date.updated2020-05-14T03:16:23Z
curtin.departmentSchool of Molecular and Life Sciences (MLS)
curtin.departmentSchool of Pharmacy and Biomedical Sciences
curtin.accessStatusFulltext not available
curtin.facultyFaculty of Science and Engineering
curtin.facultyFaculty of Health Sciences
curtin.contributor.orcidArrigan, Damien [0000-0002-1053-1273] [0000-0002-1634-5498]
curtin.contributor.orcidMancera, Ricardo [0000-0002-9191-5622]
curtin.contributor.orcidHackett, Mark [0000-0002-3296-7270]
curtin.contributor.orcidFelisilda, Bren [0000-0002-1340-902X]
curtin.contributor.orcidArrigan, Damien [0000-0002-1053-1273]
curtin.contributor.researcheridArrigan, Damien [A-7440-2010]
dcterms.source.eissn1520-5827
curtin.contributor.scopusauthoridArrigan, Damien [7004238830]
curtin.contributor.scopusauthoridArooj, Mahreen [35486823600]
curtin.contributor.scopusauthoridMancera, Ricardo [6701849195]
curtin.contributor.scopusauthoridHackett, Mark [35240056500]


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