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• W2081024414 abstract "Influenza A virus H1N1 causes human influenza (flu) in 2009. Some strains of H1N1 are endemic in humans and cause a small fraction of all influenza-like illness and a small fraction of all seasonal influenza. Zanamivir which blocks the function of the viral neuraminidase protein of influenza A virus H1N1, thus preventing the virus from reproducing by budding from the host cell has been reported for having resistance against the virus. The neuraminidase enzyme is a glycoside hydrolase enzyme which is found on the surface. It enables the virus to be released from the host cell and cleave sialic acid groups from glycoproteins and is required for influenza virus replication. The World Health Organization declared the H1N1 influenza pandemic on August 10, 2010. The present work focuses on the in silico virtual screening and molecular docking analysis for potential neuraminidase inhibitors using zanamivir like molecules retrieved from the ZINC database. The zanamivir like molecules were further inspected for PASS prediction and ADME-Toxicity analysis using in silico approaches. Molecular docking results suggest ZINC01696606, ZINC05069324 and ZINC02468939 have better binding affinity than zanamivir and better pharmacological parameters than zanamivir. Zanamivir like molecules viz. ZINC01696606, ZINC05069324 and ZINC02468939 support experimental testingas zanamivir is reported for having resistance against neuraminidase enzyme and bioavailability problems." @default.
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• W2081024414 date "2013-09-01" @default.
• W2081024414 modified "2023-09-26" @default.
• W2081024414 title "Virtual screening on potential neuraminidase inhibitors of influenza A virus H1N1" @default.
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• W2081024414 doi "https://doi.org/10.1016/j.dit.2013.06.005" @default.
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