About: Molecular simulation study of the binding mechanism of [α-PTi(2)W(10)O(40)](7−) for its promising broad-spectrum inhibitory activity to FluV-A neuraminidase

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About: Molecular simulation study of the binding mechanism of [α-PTi(2)W(10)O(40)](7−) for its promising broad-spectrum inhibitory activity to FluV-A neuraminidase Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Molecular simulation study of the binding mechanism of [α-PTi(2)W(10)O(40)](7−) for its promising broad-spectrum inhibitory activity to FluV-A neuraminidase
Creator	Hu, Donghua Wang, Jianping Zhongmin, S
topic	covid:47607c06b9a109c4a5d6f1c51fdc9db107a48bab#this
Source	Medline; PMC
abstract	Polyoxometalate (POM) has promising antiviral activities. It shows broad-spectrum inhibiting ability, high efficiency, and low toxicity. Experimental assays show that titanium containing polyoxotungstates have anti-influenza-virus activity. In this paper, the binding mechanisms of five isomers of di-Ti-substituted polyoxotungstate, [α-1,2-PTi(2)W(10)O(40)](7−) (α-1,2), [α-1,6-PTi(2)W(10)O(40)](7−) (α-1,6), [α-1,5-PTi(2)W(10)O(40)](7−) (α-1,5), [α-1,4-PTi(2)W(10)O(40)](7−) (α-1,4) and [α-1,11-PTi(2)W(10)O(40)](7−) (α-1,11), to five subtypes of influenza virus A neuraminidase (FluV-A NA) were investigated in the context of aqueous solution by using molecular docking and molecular dynamics studies. The results show that the isomer α-1,2 is superior to other isomers as a potential inhibitor to neuraminidase. The positively charged arginine residues around the active site of NA could be induced by negatively charged POM to adapt themselves and could form salt bridge interactions and hydrogen bond interactions with POM. The binding free energies of POM/NA complexes range from −5.36 to −8.31 kcal mol(−1). The electrostatic interactions are found to be the driving force during the binding process of POM to NA. The conformational analysis shows that POM tends to bind primarily with N1 and N8 at the edge of the active pocket, which causes the conformational change of the pincers structure comprising residue 347 and loop 150. Whereas, the active pockets of N2, N9 and N4 are found to be more spacious, which allows POM to enter into the active pockets directly and anchor there firmly. This study shows that negatively charged ligand as POM could induce the reorganization of the active site of NA and highlights POM as a promising inhibitor to NA despite the ever increasing mutants of NA. ELECTRONIC SUPPLEMENTARY MATERIAL: Supplementary material is available for this article at 10.1007/s11434-010-3271-8 and is accessible for authorized users.
has issue date	2010-08-14(xsd:dateTime)
bibo:doi	10.1007/s11434-010-3271-8
bibo:pmid	32214733
has license	no-cc
sha1sum (hex)	47607c06b9a109c4a5d6f1c51fdc9db107a48bab
schema:url	https://doi.org/10.1007/s11434-010-3271-8
resource representing a document's title	Molecular simulation study of the binding mechanism of [α-PTi(2)W(10)O(40)](7−) for its promising broad-spectrum inhibitory activity to FluV-A neuraminidase
has PubMed Central identifier	PMC7089260
has PubMed identifier	32214733
schema:publication	Chin Sci Bull
resource representing a document's body	covid:47607c06b9a109c4a5d6f1c51fdc9db107a48bab#body_text
is http://vocab.deri.ie/void#inDataset of	https://covidontheweb.inria.fr:4443/about/id/http/ns.inria.fr/covid19/47607c06b9a109c4a5d6f1c51fdc9db107a48bab
is schema:about of	named entity 'PTI' named entity 'residue' named entity 'kcal' named entity 'conformational change' named entity 'POM' named entity 'BINDING' named entity 'INFLUENZA VIRUS A NEURAMINIDASE' named entity 'RESIDUE' named entity 'INDUCE' named entity 'CONTEXT' named entity '2C6' named entity 'INFLUENZA-VIRUS' named entity 'AQUEOUS SOLUTION' named entity 'STRUCTURE' named entity 'CONFORMATIONAL CHANGE' named entity 'DRIVING' named entity 'FREE' named entity 'PAPER' named entity 'ELECTROSTATIC' named entity 'POTENTIAL' named entity 'SPECTRUM' named entity 'ANTIVIRAL' named entity 'COMPLEXES' named entity 'STUDIES' named entity 'USING' named entity 'HAVE' named entity 'NEGATIVELY CHARGED' named entity 'KCAL' named entity 'MOL' named entity '150' named entity 'NEURAMINIDASE' named entity 'SIMULATION' named entity 'INVESTIGATED' named entity '2C4' named entity 'MECHANISMS' named entity 'ISOMERS' named entity 'INHIBITING' named entity 'BROAD' named entity 'INHIBITORY ACTIVITY' named entity 'ADAPT' named entity 'BIND' named entity 'HYDROGEN BOND' named entity 'EXPERIMENTAL' named entity 'LOOP' named entity 'STUDY' named entity 'MOLECULAR' named entity 'ARTICLE' named entity 'MECHANISM' named entity 'ITS' named entity 'SUPERIOR' named entity 'INCREASING' named entity 'POSITIVELY CHARGED' named entity 'STUDY' named entity 'NEURAMINIDASE' named entity 'FIRMLY' named entity 'COULD BE' named entity 'BINDING' named entity 'PTI' named entity 'ANALYSIS' named entity 'MOLECULAR DOCKING' named entity 'INHIBITOR' named entity 'SALT BRIDGE' named entity 'ALLOWS' named entity 'LOW TOXICITY' named entity 'REORGANIZATION' named entity 'HIGH EFFICIENCY' named entity '2C5' named entity 'CONTAINING' named entity 'DIRECTLY' named entity 'RESULTS' named entity 'RANGE' named entity 'PINCERS' named entity 'MUTANTS' named entity 'FORCE' named entity 'ACTIVE' named entity 'FORM' named entity 'ACTIVITIES'

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