About: Promising inhibitors of main protease of novel corona virus to prevent the spread of COVID-19 using docking and molecular dynamics simulation

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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	Promising inhibitors of main protease of novel corona virus to prevent the spread of COVID-19 using docking and molecular dynamics simulation
Creator	Kumar, Dhiraj Patel, Rajan Chandra, Ramesh Dass, Sujata Jayaraj, Abhilash Kumar, Durgesh Kumar, Vinod Kumari, Kamlesh Singh, Prashant Kumar Ramappa, Venkatesh Kumar Vishvakarma, Vijay
Source	Medline; PMC
abstract	Coronavirus disease-2019 (COVID-19) is a global health emergency and the matter of serious concern, which has been declared a pandemic by WHO. Till date, no potential medicine/ drug is available to cure the infected persons from SARS-CoV-2. This deadly virus is named as novel 2019-nCoV coronavirus and caused coronavirus disease, that is, COVID-19. The first case of SARS-CoV-2 infection in human was confirmed in the Wuhan city of the China. COVID-19 is an infectious disease and spread from man to man as well as surface to man . In the present work, in silico approach was followed to find potential molecule to control this infection. Authors have screened more than one million molecules available in the ZINC database and taken the best two compounds based on binding energy score. These lead molecules were further studied through docking against the main protease of SARS-CoV-2. Then, molecular dynamics simulations of the main protease with and without screened compounds were performed at room temperature to determine the thermodynamic parameters to understand the inhibition. Further, molecular dynamics simulations at different temperatures were performed to understand the efficiency of the inhibition of the main protease in the presence of the screened compounds. Change in energy for the formation of the complexes between the main protease of novel coronavirus and ZINC20601870 as well ZINC00793735 at room temperature was determined on applying MM-GBSA calculations. Docking and molecular dynamics simulations showed their antiviral potential and may inhibit viral replication experimentally. Communicated by Ramaswamy H. Sarma
has issue date	2020-06-22(xsd:dateTime)
bibo:doi	10.1080/07391102.2020.1779131
bibo:pmid	32567995
has license	no-cc
sha1sum (hex)	9002f4d61a84e1cd9bd675f3a7eab525890eb157
schema:url	https://doi.org/10.1080/07391102.2020.1779131
resource representing a document's title	Promising inhibitors of main protease of novel corona virus to prevent the spread of COVID-19 using docking and molecular dynamics simulation
has PubMed Central identifier	PMC7332863
has PubMed identifier	32567995
schema:publication	J Biomol Struct Dyn
resource representing a document's body	covid:9002f4d61a84e1cd9bd675f3a7eab525890eb157#body_text
is schema:about of	named entity 'molecule' named entity 'antiviral' named entity 'infectious disease' named entity 'SARS-CoV-2' named entity 'protease' named entity 'binding affinity' named entity 'van der Waals' named entity 'Replica exchange' named entity 'coronavirus' named entity 'small molecule' named entity 'SARS-CoV-2' named entity 'bioavailability' named entity 'RNA' named entity 'binding site' named entity 'ZINC database' named entity '1.2' named entity 'B3LYP' named entity 'SARS-CoV-2' named entity 'free energy calculation' named entity 'viruses' named entity 'web server' named entity 'single-stranded RNA' named entity 'angiotensin-converting enzyme' named entity 'web server' named entity 'protease' named entity 'coronavirus' named entity 'RMSD' named entity 'protease' named entity 'binding affinity' named entity 'amino acids' named entity 'proteolysis' named entity 'RMSD' named entity 'RMSD' named entity 'binding energies' named entity 'protease' named entity 'receptor' named entity 'WHO' named entity 'Physiochemical' named entity 'RMSD' named entity 'entire proteins' named entity 'protease' named entity 'binding affinity' named entity 'receptor' named entity 'protease' named entity 'protease' named entity 'SARS-CoV-2' named entity '10.31' named entity 'virus' named entity 'coronavirus' named entity 'isothermally' named entity 'protease' named entity 'gastrointestinal' named entity 'protease' named entity 'coronavirus' named entity 'SARS-CoV-2' named entity 'RMSF' named entity 'protease' named entity 'Coronavirus disease' named entity 'COVID' named entity 'Pola' named entity 'virus' named entity 'Binding energy' named entity 'SARS-CoV-2' named entity 'protease' named entity 'RMSF' named entity 'enthalpy' named entity 'lungs' named entity 'coronavirus' named entity 'drug molecules' named entity 'Molecular mechanics' named entity 'root mean square deviation'

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