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    Characterization of Protein-Facilitated Ion-Transfer Mechanism at a Polarized Aqueous/Organic Interface

    Access Status
    Fulltext not available
    Authors
    Arooj, Mahreen
    Arrigan, Damien
    Mancera, Ricardo
    Date
    2019
    Type
    Journal Article
    
    Metadata
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    Citation
    Arooj, M. and Arrigan, D.W.M. and Mancera, R.L. 2019. Characterization of Protein-Facilitated Ion-Transfer Mechanism at a Polarized Aqueous/Organic Interface. Journal of Physical Chemistry B. 123 (34): pp. 7436-7444.
    Source Title
    Journal of Physical Chemistry B
    DOI
    10.1021/acs.jpcb.9b04746
    ISSN
    1520-6106
    Faculty
    Faculty of Health Sciences
    Faculty of Science and Engineering
    School
    School of Pharmacy and Biomedical Sciences
    School of Molecular and Life Sciences (MLS)
    URI
    http://hdl.handle.net/20.500.11937/79102
    Collection
    • Curtin Research Publications
    Abstract

    © 2019 American Chemical Society.

    Protein electrochemistry studies at a polarized interface between two immiscible electrolyte solutions (ITIES) indicate that the detection mechanism of a protein at the interface involves a combination of protein-anion complexation and interfacial adsorption processes. A detailed characterization of the protein-facilitated mechanism of ion transfer at the ITIES will allow the development of new label-free biomolecular detection tools. Molecular dynamics simulations were performed to describe the mechanism of transfer of the hydrophobic anion tetraphenylborate (TPB-) from a 1,2-dichloroethane (organic) phase to an aqueous phase mediated by lysozyme as a model protein under the action of an external electric field. The anion migrated to the protein at the interface and formed multiple contacts. The side chains of positively charged Lys and Arg residues formed electrostatic interactions with the anion. Nonpolar residues like Trp, Met, and Val formed hydrophobic contacts with the anion as it moved along the protein surface. During this process, lysozyme adopted multiple, partially unfolded conformations at the interface, all involving various anion-protein complexes with small free-energy barriers between them. The general mechanism of protein-facilitated ion transfer at a polarized liquid-liquid interface thus likely involves the movement of a hydrophobic anion along the protein surface through a combination of electrostatic and hydrophobic interactions.

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