About: Possibility of HIV-1 protease inhibitors-clinical trial drugs as repurposed drugs for SARS-CoV-2 main protease: a molecular docking, molecular dynamics and binding free energy simulation study

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About: Possibility of HIV-1 protease inhibitors-clinical trial drugs as repurposed drugs for SARS-CoV-2 main protease: a molecular docking, molecular dynamics and binding free energy simulation study 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
title	Possibility of HIV-1 protease inhibitors-clinical trial drugs as repurposed drugs for SARS-CoV-2 main protease: a molecular docking, molecular dynamics and binding free energy simulation study
Creator	Ancy, Iruthayaraj Kumaradhas, Poomani Sivanandam, Mugudeeswaran
source	Medline; PMC
abstract	Initially, the SARS-CoV-2 virus was emerged from Wuhan, China and rapidly spreading across the world and urges the scientific community to develop antiviral therapeutic agents. Among several strategies, drug repurposing will help to react immediately to overcome the COVID-19 pandemic. In the present study, we have chosen two clinical trial drugs against HIV-1 protease namely, TMB607 and TMC310911 to use as the inhibitors of SARS-CoV-2 main protease (M(pro)) enzyme. To make use of these two inhibitors as the repurposed drugs for COVID-19, it is essential to know the molecular basis of the binding mechanism of these two molecules with the SARS-CoV-2 M(pro). To understand the binding mechanism, we have performed molecular docking, molecular dynamics (MD) simulations, and binding free energy calculations against the SARS-CoV-2 M(pro). The docking results indicate that both molecules form intermolecular interactions with the active site amino acids of M(pro) enzyme. However, during the MD simulations, TMB607 forms strong interaction with the key amino acids of M(pro), and remains intact. The RMSD and RMSF values of both complexes were stable throughout the MD simulations. The MM-GBSA binding free energy values of both complexes are −43.7 and −34.9 kcal/mol, respectively. This in silico study proves that the TMB607 molecule binds strongly with the SARS-CoV-2 M(pro) enzyme and it may be suitable for the drug repurposing of COVID-19 and further drug designing. Communicated by Ramaswamy H. Sarma
has issue date	2020-07-06(xsd:dateTime)
bibo:doi	10.1080/07391102.2020.1786459
bibo:pmid	32627689
has license	no-cc
sha1sum (hex)	0438a5f124948475ed46fd5530472f3cac2a8486
schema:url	https://doi.org/10.1080/07391102.2020.1786459
resource representing a document's title	Possibility of HIV-1 protease inhibitors-clinical trial drugs as repurposed drugs for SARS-CoV-2 main protease: a molecular docking, molecular dynamics and binding free energy simulation study
has PubMed Central identifier	PMC7441795
has PubMed identifier	32627689
schema:publication	Journal of biomolecular structure & dynamics
resource representing a document's body	covid:0438a5f124948475ed46fd5530472f3cac2a8486#body_text
is schema:about of	named entity 'pro' named entity 'COVID-19' named entity 'docking' named entity 'stable' named entity 'simulations' »more»

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