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The H1N1 pandemic in 2009 and the H5N1 outbreak in 2005 have shocked the world as millions of people were infected and hundreds of thousands died due to the infections by the influenza virus. Oseltamivir, the most common drug to block the viral life cycle by inhibiting neuraminidase (NA) enzyme, has been less effective in some resistant cases due to the virus mutation. Presently, the binding of 10 chalcone derivatives towards H5N1 and H1N1 NAs in the non-catalytic and catalytic sites was studied using molecular docking. The in silico study was also conducted for its drug-like likeness such as Lipinski Rule, mutagenicity, toxicity and pharmacokinetic profiles. The result demonstrates that two chalcones ( 1c  and  2b ) have the potential for future NA inhibitor development. Compound  1c  inhibits H5N1 NA and H1N1 NA with IC 50  of 27.63 µM and 28.11 µM, respectively, whereas compound  2b  inhibits NAs with IC 50  of 87.54 µM and 73.17 µM for H5N1 and H1N1, respectively. The in silico drug-like likeness prediction reveals that  1c  is 62% better than  2b  (58%) in meeting the criteria. The results suggested that  1c  and  2b  have potencies to be developed as non-competitive inhibitors of neuraminidase for the future development of anti-influenza drugs.   Supplementary Information  The online version contains supplementary material available at 10.1186/s13765-021-00639-w.

A study on catalytic and non-catalytic sites of H5N1 and H1N1 neuraminidase as the target for chalcone inhibitors