Molecular docking investigation for Indonesian H274Y mutant neuraminidase type 1 with neuraminidase inhibitors

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dc.contributor.authorHerlambang, Sigit J.
dc.contributor.authorSaleh, Rosari
dc.date.accessioned2016-10-24T06:04:16Z
dc.date.available2016-10-24T06:04:16Z
dc.date.issued2012-01
dc.description.abstractThe aim of this study is to get insight the interaction between Indonesian H274Y mutant neuraminidase with four inhibitors. Not only to seek preferable inhibitor to be used, but also to investigate the interaction occurred, especially hydrogen bonds formed. Hydrogen bonds analysis and its interaction energies calculation showed that zanamivir is the most preferable inhibitor with 13 hydrogen bonds formed and –439.96 kcal/mol. Laninamivir would be an alternative inhibitor since it has 10 hydrogen bonds and –307.19 kcal/mol. The investigation of ΔSAS showed almost all active site residues buried when interacted with inhibitors. Only a few residues have an increases ΔSAS. Lipinski rule analysis showed that zanamivir and laninamivir would be best taken by injection or inhalation.en_US
dc.identifier.citationAmerican Journal of Molecular Biology, 2012, 2, 49-59en_US
dc.identifier.urihttp://dx.doi.org/10.4236/ajmb.2012.21006
dc.identifier.urihttp://hdl.handle.net/123456789/989
dc.language.isoenen_US
dc.publisherScientific Research Publishingen_US
dc.subjectMolecular Dockingen_US
dc.subjectNeuraminidaseen_US
dc.subjectInhibitoren_US
dc.subjectResistanceen_US
dc.titleMolecular docking investigation for Indonesian H274Y mutant neuraminidase type 1 with neuraminidase inhibitorsen_US
dc.typeArticleen_US
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