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    A Supramolecular Ice Growth Inhibitor

    246063_246063.pdf (22.24Mb)
    Access Status
    Open access
    Authors
    Drori, R.
    Li, C.
    Hu, C.
    Raiteri, P.
    Rohl, Andrew
    Ward, M.
    Kahr, B.
    Date
    2016
    Type
    Journal Article
    
    Metadata
    Show full item record
    Citation
    Drori, R. and Li, C. and Hu, C. and Raiteri, P. and Rohl, A. and Ward, M. and Kahr, B. 2016. A Supramolecular Ice Growth Inhibitor. Journal of the American Chemical Society. 138 (40): pp. 13396-13401.
    Source Title
    Journal of the American Chemical Society
    DOI
    10.1021/jacs.6b08267
    School
    Curtin Institute for Computation
    Funding and Sponsorship
    http://purl.org/au-research/grants/arc/FT130100463
    http://purl.org/au-research/grants/arc/DP140101776
    Remarks

    This document is the Accepted Manuscript version of a Published Work that appeared in final form in Journal of the American Chemical Society, copyright © American Chemical Society, after peer review and technical editing by the publisher. To access the final edited and published work see http://doi.org/10.1021/jacs.6b08267, see http://pubs.acs.org/page/policy/articlesonrequest/index.html.

    URI
    http://hdl.handle.net/20.500.11937/12679
    Collection
    • Curtin Research Publications
    Abstract

    Safranine O, a synthetic dye, was found to inhibit growth of ice at millimolar concentrations with an activity comparable to that of highly evolved antifreeze glycoproteins. Safranine inhibits growth of ice crystals along the crystallographic a-axis, resulting in bipyramidal needles extended along the <0001> directions as well as and plane-specific thermal hysteresis (TH) activity. The interaction of safranine with ice is reversible, distinct from the previously reported behavior of antifreeze proteins. Spectroscopy and molecular dynamics indicate that safranine forms aggregates in aqueous solution at micromolar concentrations. Metadynamics simulations and aggregation theory suggested that as many as 30 safranine molecules were preorganized in stacks at the concentrations where ice growth inhibition was observed. The simulations and single-crystal X-ray structure of safranine revealed regularly spaced amino and methyl substituents in the aggregates, akin to the ice-binding site of antifreeze proteins. Collectively, these observations suggest an unusual link between supramolecular assemblies of small molecules and functional proteins.

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