Methyl α-glycoside of N-thioacetyl-d-neuraminic acid: a potential inhibitor of influenza A virus a 1H NMR study
The binding of influenza A virus hemagglutinin to its cell surface receptor, α-linked 5-N-acetylneuraminic acid (sialic acid), was studied in solution. The effect of structural modifications introduced into the N-acetyl group of the sialic acid on the binding was monitored by determining the dissoci...
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| Hauptverfasser: | , , , , , , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
November 08, 1993
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| In: |
FEBS letters
Year: 1993, Jahrgang: 334, Heft: 1, Pages: 117-120 |
| ISSN: | 1873-3468 |
| DOI: | 10.1016/0014-5793(93)81694-U |
| Online-Zugang: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1016/0014-5793(93)81694-U Verlag, lizenzpflichtig, Volltext: https://onlinelibrary.wiley.com/doi/abs/10.1016/0014-5793%2893%2981694-U 
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| Verfasserangaben: | Daisy Machytka, Igor Kharitonenkov, Rainer Isecke, Peter Hetterich, Reinhard Brossmer, Roger A Klein, Hans-Dieter Klenk, Heinz Egge |
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| 520 | |a The binding of influenza A virus hemagglutinin to its cell surface receptor, α-linked 5-N-acetylneuraminic acid (sialic acid), was studied in solution. The effect of structural modifications introduced into the N-acetyl group of the sialic acid on the binding was monitored by determining the dissociation constants by proton nuclear magnetic resonance (1H NMR) spectroscopy. Methyl α-glycoside of N-thioacetylneuraminic acid showed high, whereas the corresponding N-methylcarbamoylneuraminic acid exhibited relatively low binding affinity towards the hemagglutinin. | ||
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