About: Virtual screening-driven drug discovery of SARS-CoV2 enzyme inhibitors targeting viral attachment, replication, post-translational modification and host immunity evasion infection mechanisms

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About: Virtual screening-driven drug discovery of SARS-CoV2 enzyme inhibitors targeting viral attachment, replication, post-translational modification and host immunity evasion infection mechanisms Goto Sponge NotDistinct Permalink

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

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Virtual screening-driven drug discovery of SARS-CoV2 enzyme inhibitors targeting viral attachment, replication, post-translational modification and host immunity evasion infection mechanisms
Creator	Wei, Dong-Qing Lim, K Allen, Justin Andrew, Mark Fernandez, Khan, Abbas Kin, Israel Liman, Alfred Luis, Agustin Macabeo, G Mark, Tristan Mendoza, O Notarte, Ong, Karsten Pastrana, Adriel Patrick, Allan Pilapil, Quimque, Rey, Arturo
Source	Medline; PMC
abstract	The novel coronavirus SARS-CoV2, the causative agent of the pandemic disease COVID-19, emerged in December 2019 forcing lockdown of communities in many countries. The absence of specific drugs and vaccines, the rapid transmission of the virus, and the increasing number of deaths worldwide necessitated the discovery of new substances for anti-COVID-19 drug development. With the aid of bioinformatics and computational modelling, ninety seven antiviral secondary metabolites from fungi were docked onto five SARS-CoV2 enzymes involved in viral attachment, replication, post-translational modification, and host immunity evasion infection mechanisms followed by molecular dynamics simulation and in silico ADMET prediction (absorption, distribution, metabolism, excretion and toxicity) of the hit compounds. Thus, three fumiquinazoline alkaloids scedapin C (15), quinadoline B (19) and norquinadoline A (20), the polyketide isochaetochromin D1 (8), and the terpenoid 11a-dehydroxyisoterreulactone A (11) exhibited high binding affinities on the target proteins, papain-like protease (PLpro), chymotrypsin-like protease (3CLpro), RNA-directed RNA polymerase (RdRp), non-structural protein 15 (nsp15), and the spike binding domain to GRP78. Molecular dynamics simulation was performed to optimize the interaction and investigate the stability of the top-scoring ligands in complex with the five target proteins. All tested complexes were found to have dynamic stability. Of the five top-scoring metabolites, quinadoline B (19) was predicted to confer favorable ADMET values, high gastrointestinal absorptive probability and poor blood-brain barrier crossing capacities. Communicated by Ramaswamy H. Sarma
has issue date	2020-06-16(xsd:dateTime)
bibo:doi	10.1080/07391102.2020.1776639
bibo:pmid	32476574
has license	no-cc
sha1sum (hex)	8cae88b61fcadb63c3a0834e501262388742eade
schema:url	https://doi.org/10.1080/07391102.2020.1776639
resource representing a document's title	Virtual screening-driven drug discovery of SARS-CoV2 enzyme inhibitors targeting viral attachment, replication, post-translational modification and host immunity evasion infection mechanisms
has PubMed Central identifier	PMC7309309
has PubMed identifier	32476574
schema:publication	J Biomol Struct Dyn
resource representing a document's body	covid:8cae88b61fcadb63c3a0834e501262388742eade#body_text
is schema:about of	named entity 'infection' named entity 'drugs' named entity 'virus' named entity 'coronavirus' named entity 'target' named entity 'host' named entity 'enzyme' named entity 'INFECTION' named entity 'BLOOD-BRAIN BARRIER' named entity 'QUINADOLINE B' named entity 'STABILITY' named entity 'CHYMOTRYPSIN-LIKE PROTEASE' named entity 'PROTEINS' named entity 'transmission' named entity 'attachment' named entity 'polymerase' named entity 'spike' named entity 'emerged' named entity 'stability' named entity 'enzymes' named entity 'All' named entity 'absorption' named entity 'simulation' named entity 'RNA-directed RNA polymerase' named entity 'stability' named entity 'absorptive' named entity 'proteins' named entity 'ligands' named entity 'pandemic' named entity 'replication' named entity 'viral' named entity 'secondary metabolites' named entity 'COVID' named entity 'metabolites' named entity 'fungi' named entity 'ADMET' named entity 'ligands' named entity 'pandemic disease' named entity 'virus' named entity 'COVID-19 drug development' named entity 'toxicity' named entity 'post-translational modification' named entity 'alkaloids' named entity '3CLpro' named entity 'probability' named entity 'enzyme inhibitors' named entity 'molecular docking' named entity 'ligands' named entity 'hydrogen bonds' named entity 'HSV' named entity 'protein' named entity 'protein crystal' named entity 'catalytic domains' named entity 'catalytic triad' named entity 'ligand' named entity 'ACE2' named entity 'kcal' named entity 'PLpro' named entity 'cellular processes' named entity 'RTP' named entity 'HSV-1' named entity 'herpes simplex virus' named entity 'SARS-CoV2'

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