| Autor: |
Nunes VS; NEQC: Núcleo de Estudos em Química Computacional, Departamento de Química, Universidade Federal de Juiz de Fora, Juiz de Fora, MG, Brasil., Paschoal DFS; NQTCM: Núcleo de Química Teórica e Computacional de Macaé, Polo Ajuda, Universidade Federal do Rio de Janeiro, Macaé, RJ, Brasil., Costa LAS; NEQC: Núcleo de Estudos em Química Computacional, Departamento de Química, Universidade Federal de Juiz de Fora, Juiz de Fora, MG, Brasil., Santos HFD; NEQC: Núcleo de Estudos em Química Computacional, Departamento de Química, Universidade Federal de Juiz de Fora, Juiz de Fora, MG, Brasil. |
| Jazyk: |
angličtina |
| Zdroj: |
Journal of biomolecular structure & dynamics [J Biomol Struct Dyn] 2022; Vol. 40 (19), pp. 8989-9003. Date of Electronic Publication: 2021 May 05. |
| DOI: |
10.1080/07391102.2021.1921033 |
| Abstrakt: |
In March 2020, the World Health Organization (WHO) declared coronavirus disease-19 (COVID-19), caused by the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), a pandemic. Since then, the search for a vaccine or drug for COVID-19 treatment has started worldwide. In this regard, a fast approach is the repurposing of drugs, primarily antiviral drugs. Herein, we performed a virtual screening using 22 antiviral drugs retrieved from the DrugBank repository, azithromycin (antibiotic), ivermectin (antinematode), and seven non-structural proteins (Nsps) of SARS-CoV-2, which are considered important targets for drugs, via molecular docking and molecular dynamics simulations. Drug-receptor binding energy was employed as the main descriptor. Based on the results, paritaprevir was predicted as a promising multi-target drug that favorably bound to all tested Nsps, mainly adipose differentiation-related protein (ADRP) (-36.2 kcal mol -1 ) and coronavirus main proteinase (Mpro) (-32.2 kcal mol -1 ). Moreover, the results suggest that simeprevir is a strong inhibitor of Mpro (-37.2 kcal mol -1 ), which is an interesting finding because Mpro plays an important role in viral replication. In addition to drug-receptor affinity, hot spot residues were characterized to facilitate the design of new drug derivatives with improved biological responses. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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