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J Enzyme Inhib Med Chem . A novel N-heterocycles substituted oseltamivir derivatives as potent inhibitors of influenza virus neuraminidase: discove

tetano

Editor, Senior Moderator
J Enzyme Inhib Med Chem


. 2023 Dec;38(1):2277135.
doi: 10.1080/14756366.2023.2277135. Epub 2023 Nov 13. A novel N-heterocycles substituted oseltamivir derivatives as potent inhibitors of influenza virus neuraminidase: discovery, synthesis and biological evaluation

Jiwei Zhang[SUP] 1 [/SUP], Chuanfeng Liu[SUP] 1 2 [/SUP], Ruifang Jia[SUP] 1 [/SUP], Xujie Zhang[SUP] 1 [/SUP], Jian Zhang[SUP] 3 [/SUP], Chiara Bertagnin[SUP] 4 [/SUP], Anna Bonomini[SUP] 4 [/SUP], Laura Guizzo[SUP] 4 [/SUP], Yuanmin Jiang[SUP] 1 [/SUP], Huinan Jia[SUP] 1 [/SUP], Shuzhen Jia[SUP] 1 [/SUP], Xiuli Ma[SUP] 5 [/SUP], Arianna Loregian[SUP] 4 [/SUP], Bing Huang[SUP] 5 [/SUP], Peng Zhan[SUP] 1 6 [/SUP], Xinyong Liu[SUP] 1 6 [/SUP]



Affiliations
Abstract

Our previous studies have shown that the introduction of structurally diverse benzyl side chains at the C5-NH[SUB]2[/SUB] position of oseltamivir to occupy 150-cavity contributes to the binding affinity with neuraminidase and anti-influenza activity. To obtain broad-spectrum neuraminidase inhibitors, we designed and synthesised a series of novel oseltamivir derivatives bearing different N-heterocycles substituents that have been proved to induce opening of the 150-loop of group-2 neuraminidases. Among them, compound 6k bearing 4-((r)-2-methylpyrrolidin-1-yl) benzyl group exhibited antiviral activities similar to or weaker than those of oseltamivir carboxylate against H1N1, H3N2, H5N1, H5N6 and H5N1-H274Y mutant neuraminidases. More encouragingly, 6k displayed nearly 3-fold activity enhancement against H3N2 virus over oseltamivir carboxylate and 2-fold activity enhancement over zanamivir. Molecular docking studies provided insights into the explanation of its broad-spectrum potency against wild-type neuraminidases. Overall, as a promising lead compound, 6k deserves further optimisation by fully considering the ligand induced flexibility of the 150-loop.

Keywords: 150-cavity; Influenza virus; drug design; neuraminidase inhibitors; oseltamivir.

 
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