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Issue 6, 2016
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Inhibition of the key enzyme of sialic acid biosynthesis by C6-Se modified N-acetylmannosamine analogs

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Abstract

Synthetically accessible C6-analogs of N-acetylmannosamine (ManNAc) were tested as potential inhibitors of the bifunctional UDP-N-acetylglucosamine-2-epimerase/N-acetylmannosamine kinase (GNE/MNK), the key enzyme of sialic acid biosynthesis. Enzymatic experiments revealed that the modification introduced at the C6 saccharide position strongly influences the inhibitory potency. A C6-ManNAc diselenide dimer showed the strongest kinase inhibition in the low μM range among all the substrates tested and successfully reduced cell surface sialylation in Jurkat cells.

Graphical abstract: Inhibition of the key enzyme of sialic acid biosynthesis by C6-Se modified N-acetylmannosamine analogs

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Publication details

The article was received on 27 okt. 2015, accepted on 13 feb. 2016 and first published on 19 feb. 2016


Article type: Edge Article
DOI: 10.1039/C5SC04082E
Chem. Sci., 2016,7, 3928-3933
  • Open access: Creative Commons BY license
    All publication charges for this article have been paid for by the Royal Society of Chemistry

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    Inhibition of the key enzyme of sialic acid biosynthesis by C6-Se modified N-acetylmannosamine analogs

    O. Nieto-Garcia, P. R. Wratil, L. D. Nguyen, V. Böhrsch, S. Hinderlich, W. Reutter and C. P. R. Hackenberger, Chem. Sci., 2016, 7, 3928
    DOI: 10.1039/C5SC04082E

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