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    Structural Changes in Insulin at a Soft Electrochemical Interface

    89417.pdf (667.4Kb)
    Access Status
    Open access
    Authors
    Lamichhane, Hum Bahadur
    Henares, Terence G
    Hackett, Mark
    Arrigan, Damien
    Date
    2021
    Type
    Journal Article
    
    Metadata
    Show full item record
    Citation
    Lamichhane, H.B. and Henares, T.G. and Hackett, M.J. and Arrigan, D.W.M. 2021. Structural Changes in Insulin at a Soft Electrochemical Interface. Analytical Chemistry. 93 (26): pp. 9094-9102.
    Source Title
    Analytical Chemistry
    DOI
    10.1021/acs.analchem.1c00657
    ISSN
    0003-2700
    Faculty
    Faculty of Science and Engineering
    School
    School of Molecular and Life Sciences (MLS)
    Remarks

    This document is the Accepted Manuscript version of a Published Work that appeared in final form in Analytical Chemistry, copyright © American Chemical Society, after peer review and technical editing by the publisher. To access the final edited and published work see https://doi.org/10.1021/acs.analchem.1c00657

    URI
    http://hdl.handle.net/20.500.11937/89593
    Collection
    • Curtin Research Publications
    Abstract

    Understanding the interaction of proteins at interfaces, which occurs at or within cell membranes and lipoprotein vesicles, is central to our understanding of protein function. Therefore, new experimental approaches to understand how protein structure is influenced by protein-interface interactions are important. Herein we build on our previous work exploring electrochemistry at the interface between two immiscible electrolyte solutions (ITIES) to investigate changes in protein secondary structure that are modulated by protein-interface interactions. The ITIES provides an experimental framework to drive protein adsorption at an interface, allowing subsequent spectroscopic analysis (e.g., Fourier transform infrared spectroscopy) to monitor changes in protein structure. Here, we reveal that the interaction between insulin and the interface destabilizes native insulin secondary structure, promoting formation of α helix secondary structures. These structural alterations result from protein-interface rather than protein-protein interactions at the interface. Although this is an emerging approach, our results provide a foundation highlighting the value of the ITIES as a tool to study protein structure and interactions at interfaces. Such knowledge may be useful to elucidate protein function within biological systems or to aid sensor development.

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