Please use this identifier to cite or link to this item: http://hdl.handle.net/10397/90272
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dc.contributorDepartment of Applied Biology and Chemical Technologyen_US
dc.creatorYe, Jen_US
dc.creatorLin, Len_US
dc.creatorXu, Jen_US
dc.creatorChan, PKSen_US
dc.creatorYang, Xen_US
dc.creatorMa, Cen_US
dc.date.accessioned2021-06-07T01:08:54Z-
dc.date.available2021-06-07T01:08:54Z-
dc.identifier.urihttp://hdl.handle.net/10397/90272-
dc.language.isoenen_US
dc.publisherMDPI AGen_US
dc.rights© 2021 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https:// creativecommons.org/licenses/by/ 4.0/).en_US
dc.rightsThe following publication Ye, J., Lin, L., Xu, J., Chan, P. K. S., Yang, X., & Ma, C. (2021). Design, Synthesis, Biological Evaluation and In Silico Studies of Pyrazole-Based NH2-Acyl Oseltamivir Analogues as Potent Neuraminidase Inhibitors. Pharmaceuticals, 14(4), 371 is available at https://doi.org/10.3390/ph14040371en_US
dc.subject150‐cavityen_US
dc.subjectInfluenza virusen_US
dc.subjectNeuraminidase inhibitoren_US
dc.subjectOseltamivir derivativesen_US
dc.subjectPyrazoleen_US
dc.titleDesign, synthesis, biological evaluation and in silico studies of pyrazole‐based NH₂‐acyl oseltamivir analogues as potent neuraminidase inhibitorsen_US
dc.typeJournal/Magazine Articleen_US
dc.identifier.volume14en_US
dc.identifier.issue4en_US
dc.identifier.doi10.3390/ph14040371en_US
dcterms.abstractOseltamivir represents one of the most successful neuraminidase (NA) inhibitors in the current anti‐influenza therapy. The 150‐cavity of NA was identified as an additional binding pocket, and novel NA inhibitors have been designed to occupy the 150‐cavity based on the structure information of oseltamivir carboxylate (OC) in complex with NA. In this study, a series of C‐5‐NH2‐acyl derivatives of OC containing the pyrazole moiety were synthesized. Several derivatives exhibited substantial inhibitory activity against NA. Moreover, in silico ADME evaluation indicated that the derivatives were drug‐like with higher oral absorption rates and greater cell permeability than OC. Additionally, molecular docking studies revealed that the derivatives interacted with both the NA enzyme active site and 150‐cavity as expected. The results provided useful information for further structural optimization of OC.en_US
dcterms.accessRightsopen accessen_US
dcterms.bibliographicCitationPharmaceuticals, Apr. 2021, v. 14, no. 4, 371en_US
dcterms.isPartOfPharmaceuticalsen_US
dcterms.issued2021-04-
dc.identifier.scopus2-s2.0-85104954282-
dc.identifier.eissn1424-8247en_US
dc.identifier.artn371en_US
dc.description.validate202106 bcvcen_US
dc.description.oaVersion of Recorden_US
dc.identifier.FolderNumbera0905-n01-
dc.identifier.SubFormID2115-
dc.description.fundingSourceRGCen_US
dc.description.fundingSourceOthersen_US
dc.description.fundingTextRGC: 15100019, C5008-19G, 14107919en_US
dc.description.pubStatusPublisheden_US
dc.description.oaCategoryCCen_US
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