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DC Field | Value | Language |
---|---|---|
dc.contributor.author | Murugesan, Sankaranarayanan | - |
dc.date.accessioned | 2023-12-11T08:36:18Z | - |
dc.date.available | 2023-12-11T08:36:18Z | - |
dc.date.issued | 2022-12 | - |
dc.identifier.uri | https://www.sciencedirect.com/science/article/pii/S0254629921004798?via%3Dihub | - |
dc.identifier.uri | http://dspace.bits-pilani.ac.in:8080/xmlui/handle/123456789/13341 | - |
dc.description.abstract | Coronaviruses (CoVs) are a large group of enveloped positive sense single-stranded RNA viruses that can cause disease to humans. These are zoonotic having potential to cause large-scale outbreaks of infections widely causing morbidity and mortality. Papain-Like Protease (PLpro) is a cysteine protease, essential for viral replication and proliferation, as a highly conserved enzyme it cleaves peptide linkage between Nsp1, Nsp2, Nsp3, and Nsp4. As a valid therapeutic target, it stops viral reproduction and boosts host immune response thereby halting further spread of infection. In the purpose of identifying inhibitors targeting Papain-Like Proteases (PLpro) we initiated a high throughput virtual screening (HTVS) protocol using a SuperNatural Database. The XP docking results revealed that two compounds SN00334175 and SN00162745 exhibited docking scores of -10.58 kcal/mol and -9.93 kcal/mol respectively. The Further PRIME MMGB-SA studies revealed Van der Waal energy and hydrophobic energy terms as major contributors for total binding free energy. The 100 ns molecular dynamics simulation of SN00334175/7JN2 and SN00162745/7JN2 revealed that these complexes were stabilized with ligand binding forming interactions with Gly266, Asn267, Tyr268, Tyr273, Thr301 and Asp302, Lys157, Leu162, Asp164, Arg166, Glu167, Pro248 and Tyr264. | en_US |
dc.language.iso | en | en_US |
dc.publisher | Elsevier | en_US |
dc.subject | Pharmacy | en_US |
dc.subject | SuperNatural Database | en_US |
dc.subject | PLpro | en_US |
dc.subject | SARS-CoV-2 | en_US |
dc.subject | Molecular docking | en_US |
dc.subject | Molecular dynamics | en_US |
dc.subject | Drug likeness | en_US |
dc.title | Identification of Papain-Like Protease inhibitors of SARS CoV-2 through HTVS, Molecular docking, MMGBSA and Molecular dynamics approach | en_US |
dc.type | Article | en_US |
Appears in Collections: | Department of Pharmacy |
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