About: Molecular docking and dynamics study of natural compound for potential inhibition of main protease of SARS-CoV-2

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About: Molecular docking and dynamics study of natural compound for potential inhibition of main protease of SARS-CoV-2 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	Molecular docking and dynamics study of natural compound for potential inhibition of main protease of SARS-CoV-2
Creator	Rahman, Islam, Ariful Amin, Al Mahmud, Shafi Zaman, Meemtaheena Abu, Mohammad Akash, Al, Shahriar Alom, Khaled, Mahmud Saleh, Md Shehab, Noor Sujon, Uddin, Raihan
Source	Medline; PMC
abstract	Newly emerged SARS-CoV-2 made recent pandemic situations across the globe is accountable for countless unwanted death and insufferable panic associated with co-morbidities among mass people. The scarcity of appropriate medical treatment and no effective vaccine or medicine against SARS-CoV-2 has turned the situation worst. Therefore, in this study, we made a deep literature review to enlist plant-derived natural compounds and considered their binding mechanism with the main protease of SARS-CoV-2 through combinatorial bioinformatics approaches. Among all, a total of 14 compounds were filtered where Carinol, Albanin, Myricetin were had better binding profile than the rest of the compounds with having binding energy of –8.476, –8.036, –8.439 kcal/mol, respectively. Furthermore, MM-GBSA calculations were also considered in this selection process to support docking studies. Besides, 100 ns molecular dynamics simulation endorsed the rigid nature, less conformational variation and binding stiffness. As this study, represents a perfect model for SARS-CoV-2 main protease inhibition through bioinformatics study, these potential drug candidates may assist the researchers to find a superior and effective solution against COVID-19 after future experiments. Communicated by Ramaswamy Sarma
has issue date	2020-07-24(xsd:dateTime)
bibo:doi	10.1080/07391102.2020.1796808
bibo:pmid	32705962
has license	no-cc
sha1sum (hex)	0833c1187dfbd67bc142195c751ac4a633bb4558
schema:url	https://doi.org/10.1080/07391102.2020.1796808
resource representing a document's title	Molecular docking and dynamics study of natural compound for potential inhibition of main protease of SARS-CoV-2
has PubMed Central identifier	PMC7441771
has PubMed identifier	32705962
schema:publication	Journal of biomolecular structure & dynamics
resource representing a document's body	covid:0833c1187dfbd67bc142195c751ac4a633bb4558#body_text
is schema:about of	named entity 'SARS-CoV-2' named entity 'mol' named entity 'pandemic' named entity 'conformational' named entity 'selection' named entity 'binding' named entity 'inhibition' named entity 'STUDIES' named entity 'CO-MORBIDITIES' named entity 'APPROPRIATE' named entity 'PEOPLE' named entity 'DEATH' named entity 'MECHANISM' named entity 'FUTURE' named entity 'VARIATION' named entity 'RECENT' named entity 'PANDEMIC' named entity 'ACROSS' named entity 'TURNED' named entity 'SUPERIOR' named entity 'GLOBE' named entity 'PROTEASE' named entity 'THEIR' named entity 'SARS-COV-2' named entity 'POTENTIAL' named entity 'PROFILE' named entity 'STUDY' named entity 'protease inhibition' named entity 'represents' named entity 'amino acid residues' named entity 'drug designing' named entity 'Mpro' named entity 'RMSD' named entity 'SASA' named entity 'protein' named entity 'carcinogenic' named entity 'hydrogen bonds' named entity 'RMSF' named entity 'molecular dynamics' named entity 'Mpro' named entity 'protease' named entity 'combinatorial' named entity 'binding energy' named entity 'superior' named entity 'medical treatment' named entity 'model' named entity 'calculations' named entity 'GBSA' named entity 'solvent accessible surface area' named entity 'single-stranded RNA' named entity 'pharmacological' named entity 'catalytic residues' named entity 'amino acid residues' named entity 'protein' named entity 'protein structure' named entity 'p-glycoprotein' named entity 'hydrophobic' named entity 'P-glycoprotein' named entity 'Myricetin' named entity 'hydrophobic' named entity 'hydrophobic' named entity 'molecular data' named entity 'Myricetin' named entity 'amino acid residues' named entity 'RMSD' named entity 'blood brain barrier' named entity 'physiological condition' named entity 'force field'

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