Abstract
Neuraminidase is an important surface glycoprotein of the influenza viruses [1]. The main role of neuraminidase is to remove the sialic acid groups from glycoproteins at the surfaces of host cells, resulting in the release of virion progeny from infected cells [2]. Diarylheptanoids, known to be abundant in A. officinarum, have been reported to have neuraminidase inhibitory activity. In this study, A. officinarum was selected as a natural resource to investigate the correlation between neuraminidase and diarylheptanoid. Four new diarylheptanoids along with 26 known diarylheptanoids were isolated from the A. officinarum extract. The molecular docking studies were performed to discover putative active binding site and corresponding binding conformation of isolated diarylheptanoids. Among the isolated diarylheptanoids, 10 compounds showed relatively stable binding energy levels in neuraminidase. Interestingly, five (11, 14, 15, 20 and 30) of these 10 compounds also showed strong inhibitory activity in neuraminidase enzyme analysis ([Fig. 1]).
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