Full metadata record
DC Field | Value | Language |
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dc.contributor.author | Das, Raju | - |
dc.contributor.author | Habiba, Sarmin Ummey | - |
dc.contributor.author | Dash, Raju | - |
dc.contributor.author | Seo, Yohan | - |
dc.contributor.author | Woo, Joohan | - |
dc.date.accessioned | 2023-07-12T10:10:18Z | - |
dc.date.available | 2023-07-12T10:10:18Z | - |
dc.date.created | 2023-03-15 | - |
dc.date.issued | 2023-02 | - |
dc.identifier.issn | 1661-6596 | - |
dc.identifier.uri | http://hdl.handle.net/20.500.11750/46115 | - |
dc.description.abstract | Shikonin, a phytochemical present in the roots of Lithospermum erythrorhizon, is well-known for its broad-spectrum activity against cancer, oxidative stress, inflammation, viruses, and anti-COVID-19 agents. A recent report based on a crystallographic study revealed a distinct conformation of shikonin binding to the SARS-CoV-2 main protease (Mpro), suggesting the possibility of designing potential inhibitors based on shikonin derivatives. The present study aimed to identify potential shikonin derivatives targeting the Mpro of COVID-19 by using molecular docking and molecular dynamics simulations. A total of 20 shikonin derivatives were screened, of which few derivatives showed higher binding affinity than shikonin. Following the MM-GBSA binding energy calculations using the docked structures, four derivatives were retained with the highest binding energy and subjected to molecular dynamics simulation. Molecular dynamics simulation studies suggested that alpha-methyl-n-butyl shikonin, beta-hydroxyisovaleryl shikonin, and lithospermidin-B interacted with two conserved residues, His41 and Cys145, through multiple bonding in the catalytic sites. This suggests that these residues may effectively suppress SARS-CoV-2 progression by inhibiting Mpro. Taken together, the present in silico study concluded that shikonin derivatives may play an influential role in Mpro inhibition. © 2023 by the authors. | - |
dc.language | English | - |
dc.publisher | MDPI | - |
dc.title | Unveiling the Potentiality of Shikonin Derivatives Inhibiting SARS-CoV-2 Main Protease by Molecular Dynamic Simulation Studies | - |
dc.type | Article | - |
dc.identifier.doi | 10.3390/ijms24043100 | - |
dc.identifier.scopusid | 2-s2.0-85149031565 | - |
dc.identifier.bibliographicCitation | International Journal of Molecular Sciences, v.24, no.4 | - |
dc.description.isOpenAccess | TRUE | - |
dc.subject.keywordAuthor | SARS-CoV-2 | - |
dc.subject.keywordAuthor | main protease | - |
dc.subject.keywordAuthor | shikonin derivatives | - |
dc.subject.keywordAuthor | molecular docking | - |
dc.subject.keywordAuthor | molecular dynamics simulation | - |
dc.subject.keywordPlus | CORONAVIRUS | - |
dc.subject.keywordPlus | DOCKING | - |
dc.subject.keywordPlus | VIRUS | - |
dc.subject.keywordPlus | COMBINATION | - |
dc.subject.keywordPlus | VACCINES | - |
dc.subject.keywordPlus | GLIDE | - |
dc.citation.number | 4 | - |
dc.citation.title | International Journal of Molecular Sciences | - |
dc.citation.volume | 24 | - |
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