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Virtual Screening of Repurposed Drugs as Potential Spike Protein Inhibitors of Different SARS-CoV-2 Variants: Molecular Docking Study.
Eweas, Ahmad F; Osman, Hosam-Eldin H; Naguib, Ibrahim A; Abourehab, Mohammed A S; Abdel-Moneim, Ahmed S.
  • Eweas AF; Department of Pharmaceutical and Medicinal Chemistry, National Research Centre, Cairo 12622, Egypt.
  • Osman HH; Department of Science, University of Technology and Applied Sciences Rustaq, Rustaq 133, Oman.
  • Naguib IA; Department of Anatomy, College of Medicine, Taif University, P.O. Box 11099, Taif 21944, Saudi Arabia.
  • Abourehab MAS; Department of Pharmaceutical Chemistry, College of Pharmacy, Taif University, P.O. Box 11099, Taif 21944, Saudi Arabia.
  • Abdel-Moneim AS; Department of Pharmaceutics, Faculty of Pharmacy, Umm Al-Qura University, Makkah 21955, Saudi Arabia.
Curr Issues Mol Biol ; 44(7): 3018-3029, 2022 Jul 04.
Article in English | MEDLINE | ID: covidwho-1917318
ABSTRACT
Like most of the RNA viruses, SARS-CoV-2 continuously mutates. Although many mutations have an insignificant impact on the virus properties, mutations in the surface protein, especially those in the receptor-binding domain, may lead to immune or vaccine escape variants, or altered binding activities to both the cell receptor and the drugs targeting such a protein. The current study intended to assess the ability of different variants of interest (VOIs) and variants of concern (VOCs) of SARS-CoV-2 for their affinities of binding to different repurposed drugs. Seven FDA approved drugs, namely, camostat, nafamostat mesylate, fenofibrate, umifenovir, nelfinavir, cefoperazone and ceftazidime, were selected based on their reported in vitro and clinical activities against SARA-CoV-2. The S1 protein subunit from eleven different variants, including the latest highly contiguous omicron variant, were used as targets for the docking study. The docking results revealed that all tested drugs possess moderate to high binding energies to the receptor-binding domain (RBD) of the S1 protein for all different variants. Cefoperazone was found to possess the highest binding energy to the RBD of the S1 protein of all the eleven variants. Ceftazidime was the second-best drug in terms of binding affinity towards the S1 RBD of the investigated variants. On the other hand, fenofibrate showed the least binding affinity towards the RBD of the S1 protein of all eleven variants. The binding affinities of anti-spike drugs varied among different variants. Most of the interacting amino acid residues of the receptor fall within the RBD (438-506).
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Full text: Available Collection: International databases Database: MEDLINE Type of study: Prognostic study Topics: Vaccines / Variants Language: English Journal: Curr Issues Mol Biol Journal subject: Molecular Biology Year: 2022 Document Type: Article Affiliation country: Cimb44070208

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Full text: Available Collection: International databases Database: MEDLINE Type of study: Prognostic study Topics: Vaccines / Variants Language: English Journal: Curr Issues Mol Biol Journal subject: Molecular Biology Year: 2022 Document Type: Article Affiliation country: Cimb44070208