A suitable drug structure for interaction with SARS‐CoV‐2 main protease between boceprevir, masitinib and rupintrivir; a molecular dynamics study

In recent years, more than 200 countries of the world have faced a health crisis due to the epidemiological disease of COVID-19 caused by the SARS-CoV-2 virus. It had a huge impact on the world economy and the global health sector. Researchers are studying the design and discovery of drugs that can...

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Detalles Bibliográficos
Autores principales: Yoosefian, Mehdi, Dashti, Razieh, Mahani, Mohamad, Montazer, Leila, Mir, Amirabbas
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Author(s). Published by Elsevier B.V. on behalf of King Saud University. 2023
Materias:
Original Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10246938/
https://www.ncbi.nlm.nih.gov/pubmed/37323221
http://dx.doi.org/10.1016/j.arabjc.2023.105051
Descripción
Sumario:In recent years, more than 200 countries of the world have faced a health crisis due to the epidemiological disease of COVID-19 caused by the SARS-CoV-2 virus. It had a huge impact on the world economy and the global health sector. Researchers are studying the design and discovery of drugs that can inhibit SARS‐CoV‐2. The main protease of SARS‐CoV‐2 is an attractive target for the study of antiviral drugs against coronavirus diseases. According to the docking results, binding energy for boceprevir, masitinib and rupintrivir with CMP are −10.80, −9.39, and −9.51 kcal/mol respectively. Also, for all investigated systems, van der Waals and electrostatic interactions are quite favorable for binding the drugs to SARS-CoV-2 coronavirus main protease, indicating confirmation of the complex stability.

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