Abstract
To probe more effective inhibitors for neuraminidase subtype N1, four potential inhibitors were synthetically designed by substitution at the C5 position of oseltamivir to provide additional interaction with the 150-cavity, a well-known active site in the neuraminidase subtype N1. Molecular docking with H5N1 and intermolecular interaction with model membrane to predict their drug effectiveness have been carried out. A comparison of four potential inhibitors with oseltamivir indicates that the glycyl derivative of oseltamivir has the most profound effects on the membrane, compared to the other derivatives. It seems to be the most promising derivative for further pharmacological evaluation as an neuraminidase inhibitor.
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