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The Enzymatic Catalysis of Neuraminidase and DeNovo Designs of Novel Inhibitors pp. 133-160 $0.00
Authors:  (Zhiwei Yang, Gang Yang, Yuangang Zu, Yujie Fu, Key Laboratory of Forest Plant Ecology, Ministry of Education, Northeast Forestry University, Harbin, P.R. China)
Abstract:
The influenza infection pandemic has spread on a world scale and become a major threat to human health. Neuraminidase (NA), a major surface glycoprotein of influenza virus with well-conserved active sites, offers an ideal target for the development of antiviral drugs. In this chapter, we will review the recent results on the NA active sites, NA-inhibitor interactions, proton transfers of NA inhibitors as well as respective roles of the core templates, functional groups and synergistic effects of NA inhibitors through the fragment approach. On such basis, the de novo designs were carried out in order to discover novel NA inhibitors as potential antiviral drugs. The calcium ion rather than conserved water molecules was found to be crucial to stabilize the NA active site; nonetheless, the conserved water molecules can greatly alter the NA-inhibitor interactions. The interaction mechanisms of NA were studied with two current antiviral drugs oseltamivir and peramivir as well as two potent lead compounds 4-(N-acetylamino)-5-guanidino-3-(3-pentyloxy) benzoic acid (BA) and 5-[(1R,2S)-1-(acetylamino)-2-methoxy-2-methylpentyl]-4-[(1Z)-1-propen-yl)-(4S,5R]-D-proline (BL). It indicated that for some NA inhibitors, for the proton transfers to form the zwitterions are not facile in aqueous solutions, which explains the low oral bioavailability of current antiviral drugs. With the fragment approach, it was revealed that the core templates rather than functional groups play a larger role during the inhibitor interactions with the NA proteins; moreover, the binding qualities are largely determined by the synergistic effects of the core templates and functional groups. 


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The Enzymatic Catalysis of Neuraminidase and DeNovo Designs of Novel Inhibitors pp. 133-160