Article ; Online: Virtual screening, ADME/T, and binding free energy analysis of anti-viral, anti-protease, and anti-infectious compounds against NSP10/NSP16 methyltransferase and main protease of SARS CoV-2.
Journal of receptor and signal transduction research
2020 Volume 40, Issue 6, Page(s) 605–612
Abstract: ... research.HighlightsNSP10/NSP16 methyltransferase and main protease complex of SARS CoV-2 bind with selected ... with our anti-viral, inti-infectious, and anti-protease compounds, which are attractive therapeutics to prevent ... drugs.NSP10/NSP16 methyltransferase and protease interacted with drugs by hydrophobic interactions ...
| Abstract | Recently, a pathogen has been identified as a novel coronavirus (SARS-CoV-2) and found to trigger novel pneumonia (COVID-19) in human beings and some other mammals. The uncontrolled release of cytokines is seen from the primary stages of symptoms to last acute respiratory distress syndrome (ARDS). Thus, it is necessary to find out safe and effective drugs against this deadly coronavirus as soon as possible. Here, we downloaded the three-dimensional model of NSP10/NSP16 methyltransferase (PDB-ID: 6w6l) and main protease (PDB-ID: 6lu7) of COVID-19. Using these molecular models, we performed virtual screening with our anti-viral, inti-infectious, and anti-protease compounds, which are attractive therapeutics to prevent infection of the COVID-19. We found that top screened compound binds with protein molecules with good dock score with the help of hydrophobic interactions and hydrogen bonding. We observed that protease complexed with Cyclocytidine hydrochloride (anti-viral and anti-cancer), Trifluridine (anti-viral), Adonitol, and Meropenem (anti-bacterial), and Penciclovir (anti-viral) bound with a good docking score ranging from -6.8 to -5.1 (Kcal/mol). Further, NSP10/NSP16 methyltransferase complexed with Telbivudine, Oxytetracycline dihydrate (anti-viral), Methylgallate (anti-malarial), 2-deoxyglucose and Daphnetin (anti-cancer) from the docking score of -7.0 to -5.7 (Kcal/mol). In conclusion, the selected compounds may be used as a novel therapeutic agent to combat this deadly pandemic disease, SARS-CoV-2 infection, but needs further experimental research.HighlightsNSP10/NSP16 methyltransferase and main protease complex of SARS CoV-2 bind with selected drugs.NSP10/NSP16 methyltransferase and protease interacted with drugs by hydrophobic interactions.Compounds show good DG binging free energy with protein complexes.Ligands were found to follow the Lipinski rule of five. |
|---|---|
| MeSH term(s) | Acyclovir/analogs & derivatives ; Acyclovir/chemistry ; Acyclovir/therapeutic use ; Ancitabine/chemistry ; Ancitabine/therapeutic use ; Antiviral Agents/chemistry ; Antiviral Agents/therapeutic use ; Betacoronavirus/drug effects ; Betacoronavirus/pathogenicity ; COVID-19 ; Coronavirus Infections/drug therapy ; Coronavirus Infections/virology ; Drug Evaluation, Preclinical ; Guanine ; Humans ; Meropenem/chemistry ; Meropenem/therapeutic use ; Models, Molecular ; Molecular Docking Simulation ; Pandemics ; Pneumonia, Viral/drug therapy ; Pneumonia, Viral/virology ; Protein Conformation/drug effects ; Ribitol/chemistry ; Ribitol/therapeutic use ; SARS-CoV-2 ; Trifluridine/chemistry ; Trifluridine/therapeutic use ; User-Computer Interface ; Viral Nonstructural Proteins/antagonists & inhibitors ; Viral Nonstructural Proteins/chemistry ; Viral Nonstructural Proteins/ultrastructure ; Viral Regulatory and Accessory Proteins/antagonists & inhibitors ; Viral Regulatory and Accessory Proteins/chemistry ; Viral Regulatory and Accessory Proteins/ultrastructure |
| Chemical Substances | Antiviral Agents ; NSP10 protein, SARS-CoV-2 ; NSP16 protein, SARS-CoV-2 ; Viral Nonstructural Proteins ; Viral Regulatory and Accessory Proteins ; penciclovir (359HUE8FJC) ; Ribitol (488-81-3) ; Guanine (5Z93L87A1R) ; Ancitabine (DO2D32W0VC) ; Meropenem (FV9J3JU8B1) ; Trifluridine (RMW9V5RW38) ; Acyclovir (X4HES1O11F) |
| Keywords | covid19 |
| Language | English |
| Publishing date | 2020-06-01 |
| Publishing country | England |
| Document type | Journal Article |
| ZDB-ID | 1230969-2 |
| ISSN | 1532-4281 ; 1079-9893 |
| ISSN (online) | 1532-4281 |
| ISSN | 1079-9893 |
| DOI | 10.1080/10799893.2020.1772298 |
| Database | MEDical Literature Analysis and Retrieval System OnLINE |
More links
Kategorien
In stock of ZB MED Cologne/Königswinter
| Zs.A 1643: Show issues | Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG) |
Order via subito
This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.