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  • Selective protein unfolding: a universal mechanism of action for the development of irreversible inhibitors

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    Author(s)
    Askin, Samuel
    Bond, Thomas EH
    Sorenson, Alanna E
    Moreau, Morgane JJ
    Antony, Helma
    Davis, Rohan A
    Schaeffer, Patrick M
    Griffith University Author(s)
    Davis, Rohan A.
    Year published
    2018
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    Abstract
    High-throughput differential scanning fluorimetry of GFP-tagged proteins (HT-DSF-GTP) was applied for the identification of novel enzyme inhibitors acting by a mechanism termed: selective protein unfolding (SPU). Four different protein targets were interrogated with the same library to identify target-selective hits. Several hits selectively destabilized bacterial biotin protein ligase. Structure–activity relationship data confirmed a structure-dependent mechanism of protein unfolding. Simvastatin and altenusin were confirmed to irreversibly inactivate biotin protein ligase. The principle of SPU combined with HT-DSF-GTP ...
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    High-throughput differential scanning fluorimetry of GFP-tagged proteins (HT-DSF-GTP) was applied for the identification of novel enzyme inhibitors acting by a mechanism termed: selective protein unfolding (SPU). Four different protein targets were interrogated with the same library to identify target-selective hits. Several hits selectively destabilized bacterial biotin protein ligase. Structure–activity relationship data confirmed a structure-dependent mechanism of protein unfolding. Simvastatin and altenusin were confirmed to irreversibly inactivate biotin protein ligase. The principle of SPU combined with HT-DSF-GTP affords an invaluable and innovative workflow for the identification of new inhibitors with potential applications as antimicrobials and other biocides.
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    Journal Title
    Chemical Communications
    Volume
    54
    Issue
    14
    DOI
    https://doi.org/10.1039/c8cc00090e
    Copyright Statement
    © The Author(s) 2018. This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial 3.0 Unported (CC BY-NC 3.0) License, which permits unrestricted, non-commercial use, distribution and reproduction in any medium, providing that the work is properly cited.
    Subject
    Chemical sciences
    Other chemical sciences not elsewhere classified
    Publication URI
    http://hdl.handle.net/10072/379894
    Collection
    • Journal articles

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