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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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
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author Yoosefian, Mehdi
Dashti, Razieh
Mahani, Mohamad
Montazer, Leila
Mir, Amirabbas
author_facet Yoosefian, Mehdi
Dashti, Razieh
Mahani, Mohamad
Montazer, Leila
Mir, Amirabbas
author_sort Yoosefian, Mehdi
collection PubMed
description 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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spelling pubmed-102469382023-06-08 A suitable drug structure for interaction with SARS‐CoV‐2 main protease between boceprevir, masitinib and rupintrivir; a molecular dynamics study Yoosefian, Mehdi Dashti, Razieh Mahani, Mohamad Montazer, Leila Mir, Amirabbas Arab J Chem Original Article 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. The Author(s). Published by Elsevier B.V. on behalf of King Saud University. 2023-09 2023-06-07 /pmc/articles/PMC10246938/ /pubmed/37323221 http://dx.doi.org/10.1016/j.arabjc.2023.105051 Text en © 2023 The Author(s) Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.
spellingShingle Original Article
Yoosefian, Mehdi
Dashti, Razieh
Mahani, Mohamad
Montazer, Leila
Mir, Amirabbas
A suitable drug structure for interaction with SARS‐CoV‐2 main protease between boceprevir, masitinib and rupintrivir; a molecular dynamics study
title A suitable drug structure for interaction with SARS‐CoV‐2 main protease between boceprevir, masitinib and rupintrivir; a molecular dynamics study
title_full A suitable drug structure for interaction with SARS‐CoV‐2 main protease between boceprevir, masitinib and rupintrivir; a molecular dynamics study
title_fullStr A suitable drug structure for interaction with SARS‐CoV‐2 main protease between boceprevir, masitinib and rupintrivir; a molecular dynamics study
title_full_unstemmed A suitable drug structure for interaction with SARS‐CoV‐2 main protease between boceprevir, masitinib and rupintrivir; a molecular dynamics study
title_short A suitable drug structure for interaction with SARS‐CoV‐2 main protease between boceprevir, masitinib and rupintrivir; a molecular dynamics study
title_sort suitable drug structure for interaction with sars‐cov‐2 main protease between boceprevir, masitinib and rupintrivir; a molecular dynamics study
topic Original Article
url 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
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