title: Molecular docking, synthesis, and biological evaluation of naphthoquinone as potential novel scaffold for H5N1 neuraminidase inhibition.
abstract: A series of dimeric naphthoquinones containing natural 2-hydroxy-1-4-naphthoquinone moiety was designed, synthesized, and evaluated against neuraminidase of H5N1 virus. p-hydroxy derivatives showed higher inhibition when compared to p-halogenated compounds. Molecular docking studies conducted with H5N1 neuraminidase clearly demonstrated different binding modes of the most active compound onto the open and closed conformations of loop 150. The results thus provide not only evidences of a novel scaffold evaluated as inhibitor, but also a rational explanation involving molecular modeling and the role of loop 150 in the binding.
authors.affiliation: a Department of Chemistry , Karunya University , Coimbatore , India.|b School of Pharmaceutical Sciences, Universiti Sains Malaysia , Penang , Malaysia.
authors.forename: Garima
authors.initials: G
authors.lastname: Sharma
authors.affiliation: a Department of Chemistry , Karunya University , Coimbatore , India.
authors.forename: S
authors.initials: S
authors.lastname: Vasanth Kumar
authors.affiliation: b School of Pharmaceutical Sciences, Universiti Sains Malaysia , Penang , Malaysia.
authors.forename: Habibah A
authors.initials: HA
authors.lastname: Wahab
mesh_terms: D001665:Binding Sites; D004791:Enzyme Inhibitors / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology; D006801:Humans; D053124:Influenza A Virus, H5N1 Subtype / Q000201:enzymology*; D062105:Molecular Docking Simulation; D015394:Molecular Structure; D009285:Naphthoquinones / Q000737:chemistry* / Q000378:metabolism / Q000494:pharmacology; D009439:Neuraminidase / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism; D000072417:Protein Domains
chemical_list: D004791:Enzyme Inhibitors; D009285:Naphthoquinones; D009439:Neuraminidase
keywords: H5N1; lawsone; molecular docking; naphthoquinone; neuraminidase