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    Secondary Structural Changes in Proteins as a Result of Electroadsorption at Aqueous-Organogel Interfaces

    Access Status
    Fulltext not available
    Authors
    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
    Date
    2019
    Type
    Journal Article
    
    Metadata
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    Citation
    Booth, 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.
    Source Title
    Langmuir
    DOI
    10.1021/acs.langmuir.8b04227
    ISSN
    0743-7463
    Faculty
    Faculty of Science and Engineering
    Faculty of Health Sciences
    School
    School of Molecular and Life Sciences (MLS)
    School of Pharmacy and Biomedical Sciences
    URI
    http://hdl.handle.net/20.500.11937/79098
    Collection
    • Curtin Research Publications
    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. ©

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