1. Aurasperone A Inhibits SARS CoV-2 In Vitro: An Integrated In Vitro and In Silico Study.
- Author
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ElNaggar MH, Abdelwahab GM, Kutkat O, GabAllah M, Ali MA, El-Metwally MEA, Sayed AM, Abdelmohsen UR, and Khalil AT
- Subjects
- Adenosine Monophosphate analogs & derivatives, Adenosine Monophosphate pharmacology, Alanine analogs & derivatives, Alanine pharmacology, Animals, Antiviral Agents isolation & purification, Aspergillus niger chemistry, Chlorocebus aethiops, Chromones isolation & purification, Coronavirus 3C Proteases metabolism, Coronavirus Papain-Like Proteases metabolism, Coronavirus RNA-Dependent RNA Polymerase metabolism, Molecular Docking Simulation, Protease Inhibitors isolation & purification, RNA Helicases metabolism, Spike Glycoprotein, Coronavirus metabolism, Vero Cells, Antiviral Agents pharmacology, Chromones pharmacology, Coronavirus 3C Proteases antagonists & inhibitors, Protease Inhibitors pharmacology, SARS-CoV-2 drug effects
- Abstract
Several natural products recovered from a marine-derived Aspergillus niger were tested for their inhibitory activity against SARS CoV-2 in vitro. Aurasperone A ( 3 ) was found to inhibit SARS CoV-2 efficiently (IC
50 = 12.25 µM) with comparable activity with the positive control remdesivir (IC50 = 10.11 µM). Aurasperone A exerted minimal cytotoxicity on Vero E6 cells (CC50 = 32.36 mM, SI = 2641.5) and it was found to be much safer than remdesivir (CC50 = 415.22 µM, SI = 41.07). To putatively highlight its molecular target, aurasperone A was subjected to molecular docking against several key-viral protein targets followed by a series of molecular dynamics-based in silico experiments that suggested Mpro to be its primary viral protein target. More potent anti-SARS CoV-2 Mpro inhibitors can be developed according to our findings presented in the present investigation.- Published
- 2022
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