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International Journal of Medicinal Chemistry
Volume 2011, Article ID 539245, 7 pages
Research Article

Evaluation of a Set of C9 N-acyl Neu5Ac2en Mimetics as Viral Sialidase Selective Inhibitors

1Department of Applied Bioorganic Chemistry, Faculty of Applied Biological Sciences, Gifu University, Gifu, Japan
2Department of Medicinal Chemistry, Ernest Mario School of Pharmacy, Rutgers, The State University of New Jersey, USA
3Faculty of Medicine, Thammasat University (Rangsit Campus), Pathumthani, Thailand
4Department of Biomedical Sciences, College of Life and Health Sciences, Chubu University, Aichi, Japan
5Cancer Glycosylation Research, Institute of Molecular Biomembrane and Glycobiology, Tohoku Pharmaceutical University, Sendai, Japan
6Institute for Integrated Cell-Material Sciences (iCeMS), Kyoto University, Japan

Received 2 October 2010; Revised 16 November 2010; Accepted 16 November 2010

Academic Editor: Giulio Rastelli

Copyright © 2011 Sadagopan Magesh et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Identification of selective influenza viral sialidase inhibitors is highly desirable in order to minimize or avoid the adverse effects due to the possible inhibition of endogenous human sialidases. We recently reported the evaluation of C9 N-acyl Neu5Ac2en mimetics as probes for human sialidases. Herein, we describe the in vitro activity of the same set of C9 N-acyl Neu5Ac2en mimetics against sialidases expressed by influenza virus A/PR/8/34 (H1N1), A/Memphis/1/72 (H3N2), and A/Duck/313/78 (H5N3) strains. Compound 8 is identified as a promising starting point for the development of viral sialidase selective inhibitors. Multiple sequence alignment and molecular docking techniques are also performed to explore the plausible interaction of compound 8 with viral sialidases.