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    Disaccharide Residues are Required for Native Antifreeze Glycoprotein Activity.

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    Author
    Sun, Yuling
    Giubertoni, Giulia
    Bakker, Huib J
    Liu, Jie
    Wagner, Manfred
    Ng, David Y W
    Devries, Arthur L
    Meister, Konrad
    Keyword
    Hydroxyls
    Modification
    Amides
    Antifreeze
    Transition temperature
    Antifreeze glycoproteins (AFGPs)
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    URI
    http://hdl.handle.net/11122/12155
    Abstract
    Antifreeze glycoproteins (AFGPs) are able to bind to ice, halt its growth, and are the most potent inhibitors of ice recrystallization known. The structural basis for AFGP’s unique properties remains largely elusive. Here we determined the antifreeze activities of AFGP variants that we constructed by chemically modifying the hydroxyl groups of the disaccharide of natural AFGPs. Using nuclear magnetic resonance, two-dimensional infrared spectroscopy, and circular dichroism, the expected modifications were confirmed as well as their effect on AFGPs solution structure. We find that the presence of all the hydroxyls on the disaccharides is a requirement for the native AFGP hysteresis as well as the maximal inhibition of ice recrystallization. The saccharide hydroxyls are apparently as important as the acetyl group on the galactosamine, the α-linkage between the disaccharide and threonine, and the methyl groups on the threonine and alanine. We conclude that the use of hydrogen-bonding through the hydroxyl groups of the disaccharide and hydrophobic interactions through the polypeptide backbone are equally important in promoting the antifreeze activities observed in the native AFGPs. These important criteria should be considered when designing synthetic mimics.
    Date
    2021-05-06
    Publisher
    ACS Publications
    Type
    Article
    Other
    Peer-Reviewed
    Yes
    Citation
    Disaccharide Residues are Required for Native Antifreeze Glycoprotein Activity Yuling Sun, Giulia Giubertoni, Huib J. Bakker, Jie Liu, Manfred Wagner, David Y. W. Ng, Arthur L. Devries, and Konrad Meister Biomacromolecules 2021 22 (6), 2595-2603 DOI: 10.1021/acs.biomac.1c00313
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    Meister, Konrad

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