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Issue 76, 2017
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Polyoxometalates as sialidase mimics: selective and non-destructive removal of sialic acid from a glycoprotein promoted by phosphotungstic acid

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Abstract

The selective hydrolysis of the glycosidic bond between the terminal sialic acid and the penultimate sugar has been achieved in the alpha-2-HS-glycoprotein (Fetuin-A) in the presence of H3PW12O40, a Keggin type polyoxometalate. A controlled liberation of sialic acid from the glycoprotein could be achieved at pH 3.0 and 37 °C without the destruction of the protein backbone.

Graphical abstract: Polyoxometalates as sialidase mimics: selective and non-destructive removal of sialic acid from a glycoprotein promoted by phosphotungstic acid

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Publication details

The article was received on 28 Jul 2017, accepted on 31 Aug 2017 and first published on 01 Sep 2017


Article type: Communication
DOI: 10.1039/C7CC05888H
Citation: Chem. Commun., 2017,53, 10600-10603
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    Polyoxometalates as sialidase mimics: selective and non-destructive removal of sialic acid from a glycoprotein promoted by phosphotungstic acid

    L. S. Van Rompuy and T. N. Parac-Vogt, Chem. Commun., 2017, 53, 10600
    DOI: 10.1039/C7CC05888H

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