| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1376284 | Bioorganic & Medicinal Chemistry Letters | 2007 | 4 Pages |
Abstract
The X-ray crystal structure of the paramyxoviral surface glycoprotein haemagglutinin-neuraminidase (HN) from Newcastle Disease virus was used as a template to design inhibitors of the HN from human parainfluenza virus type-3 (hPIV-3). 4-O-Alkylated derivatives of 2-deoxy-2,3-didehydro-N-acetylneuraminic acid (Neu5Ac2en), accessed from 8,9-O-isopropylidenated-Neu5Ac2en1Me, were found to inhibit the sialidase (neuraminidase) activity of hPIV-3 (strain C243) in the range of 3–30 μM. This is comparable or improved activity compared to the parent 4-hydroxy compound.
Graphical abstract4-O-Alkylated Neu5Ac2en derivatives display micromolar inhibition of hPIV-3 sialidase activity.Figure optionsDownload full-size imageDownload as PowerPoint slide
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Physical Sciences and Engineering
Chemistry
Organic Chemistry
Authors
David J. Tindal, Jeffrey C. Dyason, Robin J. Thomson, Takashi Suzuki, Hiroo Ueyama, Yohta Kuwahara, Naoyoshi Maki, Yasuo Suzuki, Mark von Itzstein,