Tags

Type your tag names separated by a space and hit enter

Potential anti-viral activity of approved repurposed drug against main protease of SARS-CoV-2: an in silico based approach.
J Biomol Struct Dyn. 2020 May 25 [Online ahead of print]JB

Abstract

The Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) which was first reported in Wuhan province of China, has become a deadly pandemic causing alarmingly high morbidity and mortality. In the absence of new targeted drugs and vaccines against SARS-CoV-2 at present, the choices for effective treatments are limited. Therefore, considering the exigency of the situation, we focused on identifying the available approved drugs as potential inhibitor against the promising Coronavirus drug target, the Main Protease, using computer-aided methods. We created a library of U. S. Food and Drug Administration approved anti-microbial drugs and virtually screened it against the available crystal structures of Main Protease of the virus. The study revealed that Viomycin showed the highest -CDocker energy after docking at the active site of SARS-CoV-2 Main Protease. It is noteworthy that Viomycin showed higher -CDocker energy as compared to the drugs currently under clinical trial for SARS-CoV-2 treatment viz. Ritonavir and Lopinavir. Additionally, Viomycin formed higher number of H-bonds with SARS-CoV-2 Main Protease than its co-crystallised inhibitor compound N3. Molecular dynamics simulation further showed that Viomycin embedded deeply inside the binding pocket and formed robust binding with SARS-CoV-2 Main Protease. Therefore, we propose that Viomycin may act as a potential inhibitor of the Main Protease of SARS-CoV-2. Further optimisations with the drug may support the much-needed rapid response to mitigate the pandemic.Communicated by Ramaswamy H. Sarma.

Authors+Show Affiliations

National Institute of Electronics and Information Technology (NIELIT), Guwahati, Guwahati, Assam, India.Model Rural Health Research Unit (MRHRU), Tripura, India.Department of Pharmaceutical Sciences, Dibrugarh University, Dibrugarh, India.Bioinformatics Infrastructure Facility, College of Veterinary Science, Assam Agricultural University, Guwahati, India.Department of Biotechnology, Royal Global University, Guwahati, India.Department of Biotechnology, Royal Global University, Guwahati, India.Department of Pharmaceutical Sciences, Dibrugarh University, Dibrugarh, India.Bioinformatics Infrastructure Facility, College of Veterinary Science, Assam Agricultural University, Guwahati, India.Department of Biotechnology, Royal Global University, Guwahati, India.Department of Biotechnology, Royal Global University, Guwahati, India.

Pub Type(s)

Letter

Language

eng

PubMed ID

32406317

Citation

Mahanta, Saurov, et al. "Potential Anti-viral Activity of Approved Repurposed Drug Against Main Protease of SARS-CoV-2: an in Silico Based Approach." Journal of Biomolecular Structure & Dynamics, 2020, pp. 1-10.
Mahanta S, Chowdhury P, Gogoi N, et al. Potential anti-viral activity of approved repurposed drug against main protease of SARS-CoV-2: an in silico based approach. J Biomol Struct Dyn. 2020.
Mahanta, S., Chowdhury, P., Gogoi, N., Goswami, N., Borah, D., Kumar, R., Chetia, D., Borah, P., Buragohain, A. K., & Gogoi, B. (2020). Potential anti-viral activity of approved repurposed drug against main protease of SARS-CoV-2: an in silico based approach. Journal of Biomolecular Structure & Dynamics, 1-10. https://doi.org/10.1080/07391102.2020.1768902
Mahanta S, et al. Potential Anti-viral Activity of Approved Repurposed Drug Against Main Protease of SARS-CoV-2: an in Silico Based Approach. J Biomol Struct Dyn. 2020 May 25;1-10. PubMed PMID: 32406317.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Potential anti-viral activity of approved repurposed drug against main protease of SARS-CoV-2: an in silico based approach. AU - Mahanta,Saurov, AU - Chowdhury,Purvita, AU - Gogoi,Neelutpal, AU - Goswami,Nabajyoti, AU - Borah,Debajit, AU - Kumar,Rupesh, AU - Chetia,Dipak, AU - Borah,Probodh, AU - Buragohain,Alak K, AU - Gogoi,Bhaskarjyoti, Y1 - 2020/05/25/ PY - 2020/5/15/pubmed PY - 2020/5/15/medline PY - 2020/5/15/entrez KW - COVID-19 KW - FDA approved drugs KW - Mpro KW - SARS-CoV-2 KW - docking KW - molecular dynamics KW - viomycin SP - 1 EP - 10 JF - Journal of biomolecular structure & dynamics JO - J. Biomol. Struct. Dyn. N2 - The Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) which was first reported in Wuhan province of China, has become a deadly pandemic causing alarmingly high morbidity and mortality. In the absence of new targeted drugs and vaccines against SARS-CoV-2 at present, the choices for effective treatments are limited. Therefore, considering the exigency of the situation, we focused on identifying the available approved drugs as potential inhibitor against the promising Coronavirus drug target, the Main Protease, using computer-aided methods. We created a library of U. S. Food and Drug Administration approved anti-microbial drugs and virtually screened it against the available crystal structures of Main Protease of the virus. The study revealed that Viomycin showed the highest -CDocker energy after docking at the active site of SARS-CoV-2 Main Protease. It is noteworthy that Viomycin showed higher -CDocker energy as compared to the drugs currently under clinical trial for SARS-CoV-2 treatment viz. Ritonavir and Lopinavir. Additionally, Viomycin formed higher number of H-bonds with SARS-CoV-2 Main Protease than its co-crystallised inhibitor compound N3. Molecular dynamics simulation further showed that Viomycin embedded deeply inside the binding pocket and formed robust binding with SARS-CoV-2 Main Protease. Therefore, we propose that Viomycin may act as a potential inhibitor of the Main Protease of SARS-CoV-2. Further optimisations with the drug may support the much-needed rapid response to mitigate the pandemic.Communicated by Ramaswamy H. Sarma. SN - 1538-0254 UR - https://www.unboundmedicine.com/medline/citation/32406317/Potential_anti_viral_activity_of_approved_repurposed_drug_against_main_protease_of_SARS_CoV_2:_an_in_silico_based_approach_ L2 - http://www.tandfonline.com/doi/full/10.1080/07391102.2020.1768902 DB - PRIME DP - Unbound Medicine ER -
Try the Free App:
Prime PubMed app for iOS iPhone iPad
Prime PubMed app for Android
Prime PubMed is provided
free to individuals by:
Unbound Medicine.