Identification of potential SARS-CoV-2 Mpro inhibitors from a Thai natural product database via interaction fingerprint-based virtual screening

Discovery of a new SARS-CoV-2 Mpro inhibitor from a natural product and natural product-like compound database using in silico and in vitro studies.

Identification of Potential SARS-CoV-2 Main Protease (MPro) Inhibitors Through Pharmacophore Modeling, Molecular Docking, and Molecular Dynamics Simulation Approaches

The findings suggest that Lig-1, followed by Lig-3, may serve as promising computational lead compounds targeting SARS-CoV-2 MPro, representing promising candidates for further experimental validation.

AI-guided Designing of SARS-CoV-2 Main Protease (M pro ) Inhibitors: An Approach for Novel Antiviral Compound Discovery

Main protease (Mpro) enzyme of Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) cleaves polyprotein pp1a and pp1ab at 11 sites, producing essential proteins of viral machinery, and possesses a conserved Cys145-His41 catalytic dyad. While different mutated strains of this virus are being identified, the...

In Silico Identification of Potent SARS-CoV-2 RdRp Inhibitors: DFT and Molecular Docking Analysis of Acylated Glucopyranoside Derivatives

The results demonstrate the promise of modified MDG derivatives as lead compounds and justify further in vitro and in vivo studies to validate their antiviral activity against SARS-CoV-2.

Natural Metabolites from Clinacanthus nutans as Promising SARS-CoV-2 Main Protease Inhibitors: Insights from Molecular Docking and Dynamics Simulations

Overall, vitexin shows promising binding characteristics as a natural compound targeting Mpro, but it does not surpass the native ligand in terms of overall binding stability, warranting further optimization and experimental validation.

Computational Identification of Shikimic Acid Derivatives as Potential SARS-CoV-2 Inhibitors: An In Silico Approach.

The docking, ADMET, and MD simulation studies indicate that the designed shikimic acid derivatives have good binding affinity and drug-like properties, and are stable in the active site of the SARS-CoV-2 main protease.