About: Unravelling lead antiviral phytochemicals for the inhibition of SARS-CoV-2 M(pro) enzyme through in silico approach

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About: Unravelling lead antiviral phytochemicals for the inhibition of SARS-CoV-2 M(pro) enzyme through in silico approach Goto Sponge NotDistinct Permalink

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

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Unravelling lead antiviral phytochemicals for the inhibition of SARS-CoV-2 M(pro) enzyme through in silico approach
Creator	Ali, Mohammad Al-Anazi, Al-Anazi, Mashay Farah, Mohammad Gurung, Arun Khalid, Mashay Lee, Joongku
source	Elsevier; Medline; PMC
abstract	A new SARS coronavirus (SARS-CoV-2) belonging to the genus Betacoronavirus has caused a pandemic known as COVID-19. Among coronaviruses, the main protease (M(pro)) is an essential drug target which, along with papain-like proteases catalyzes the processing of polyproteins translated from viral RNA and recognizes specific cleavage sites. There are no human proteases with similar cleavage specificity and therefore, inhibitors are highly likely to be nontoxic. Therefore, targeting the SARS-CoV-2 M(pro) enzyme with small molecules can block viral replication. The present study is aimed at the identification of promising lead molecules for SARS-CoV-2 M(pro) enzyme through virtual screening of antiviral compounds from plants. The binding affinity of selected small drug-like molecules to SARS-CoV-2 M(pro), SARS-CoV M(pro) and MERS-CoV M(pro) were studied using molecular docking. Bonducellpin D was identified as the best lead molecule which shows higher binding affinity (−9.28 kcal/mol) as compared to the control (−8.24 kcal/mol). The molecular binding was stabilized through four hydrogen bonds with Glu166 and Thr190 as well as hydrophobic interactions via eight residues. The SARS-CoV-2 M(pro) shows identities of 96.08% and 50.65% to that of SARS-CoV M(pro) and MERS-CoV M(pro) respectively at the sequence level. At the structural level, the root mean square deviation (RMSD) between SARS-CoV-2 M(pro) and SARS-CoV M(pro) was found to be 0.517 Å and 0.817 Å between SARS-CoV-2 M(pro) and MERS-CoV M(pro). Bonducellpin D exhibited broad-spectrum inhibition potential against SARS-CoV M(pro) and MERS-CoV M(pro) and therefore is a promising drug candidate, which needs further validations through in vitro and in vivo studies.
has issue date	2020-05-22(xsd:dateTime)
bibo:doi	10.1016/j.lfs.2020.117831
bibo:pmid	32450166
has license	no-cc
sha1sum (hex)	7b4c3e4a3a3c9c8712db2a3b46c12a89412ebe16
schema:url	https://doi.org/10.1016/j.lfs.2020.117831
resource representing a document's title	Unravelling lead antiviral phytochemicals for the inhibition of SARS-CoV-2 M(pro) enzyme through in silico approach
has PubMed Central identifier	PMC7243810
has PubMed identifier	32450166
schema:publication	Life Sci
resource representing a document's body	covid:7b4c3e4a3a3c9c8712db2a3b46c12a89412ebe16#body_text
is schema:about of	named entity 'pro' named entity 'higher' named entity 'Neuraminidase inhibitors' named entity 'Simeprevir' named entity 'Zanamivir' named entity 'selected' named entity 'COVID-19' named entity 'pro' named entity 'Journal' named entity 'structural level' named entity 'Acyclovir' named entity 'belonging' named entity 'highly' named entity 'Betacoronavirus' named entity 'inhibitors' named entity 'enzyme' named entity 'antiviral' named entity 'APPROVED' named entity 'ENZYME' named entity 'DRUG TARGET' named entity 'NEEDS' named entity 'SPECIFICITY' named entity 'ROOT MEAN SQUARE' named entity 'SELECTED' named entity 'LIKE' named entity 'IDENTIFIED' named entity 'PRO' named entity 'HIGHER' named entity 'BINDING AFFINITY' named entity 'MAJORITY' named entity 'INHIBITION CONSTANT' named entity 'TABLE' named entity 'MOLECULE' named entity 'PAPAIN' covid:arg/7b4c3e4a3a3c9c8712db2a3b46c12a89412ebe16 named entity 'inhibition' named entity 'Boceprevir' named entity 'cleavage' named entity 'Nevirapine' named entity 'nontoxic' named entity 'HCV' named entity 'polyproteins' named entity 'protease inhibitors' named entity 'pro' named entity 'mol' named entity 'SARS-CoV' named entity 'pro' named entity 'phytochemicals' named entity 'cleavage' named entity 'genus' named entity 'binding affinity' named entity 'Nelfinavir' named entity 'viral replication' named entity 'SARS-CoV' named entity 'kinase' named entity 'specific' named entity 'SARS-CoV-2' named entity 'pro' named entity 'The' named entity 'Simeprevir' named entity 'mol' named entity 'proteases' named entity 'kcal' named entity 'recognizes' named entity 'SARS-CoV-2' named entity 'kcal' named entity 'antiviral drugs' named entity 'Oseltamivir' named entity 'stabilized' named entity 'Lopinavir' named entity 'phytochemicals' named entity 'protease' named entity 'small molecules' named entity 'Nelfinavir' named entity 'catalyzes'

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