ArticleProteins2022
Crystal-structures-guided design of fragment-based drugs for inhibiting the main protease of SARS-CoV-2.
Article in Proteins, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 10 citations in OpenAlex.
- Advances in Fragment-based Drug Design: Lessons and Innovations from the Post-COVID Drug Discovery Landscape.Mini reviews in medicinal chemistry · 2026Review
- Computational Insights into Acrylamide Fragment Inhibition of SARS-CoV-2 Main Protease.Current issues in molecular biology · 2024Article
- Molecular Integrative Study on Inhibitory Effects of Pentapeptides on Polymerization and Cell Toxicity of Amyloid-β Peptide (1-42).Current issues in molecular biology · 2024Article
- Synthesis and In Silico Investigation of Isatin-Based Schiff Bases as Potential Inhibitors for Promising Targets against SARS-CoV-2.ChemistrySelect · 2022Article
- Integrated bioinformatics-cheminformatics approach toward locating pseudo-potential antiviral marine alkaloids against SARS-CoV-2-Mpro.Proteins · 2022Article
- Crystal-structures-guided design of fragment-based drugs for inhibiting the main protease of SARS-CoV-2.Proteins · 2022Article
- Fragment-based in silico design of SARS-CoV-2 main protease inhibitors.Chemical biology & drug design · 2021Article
- Structural Basis of Potential Inhibitors Targeting SARS-CoV-2 Main Protease.Frontiers in chemistry · 2021Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Since the beginning of the COVID-19 pandemic, scientists across the globe are racing to find a cure for the highly contagious infectious disease caused by the SARS-CoV-2 virus. Despite many promising ongoing progress, there are currently no FDA approved drug to treat infected patients. Recently, the crowdsourcing of drug discovery for inhibiting the main protease (Mpro) of SARS-CoV-2 have yielded a plenty of drug fragments resolved inside the active site of Mpro via the crystallography method. Following the principle of fragment-based drug design (FBDD), we are motivated to design a potent drug candidate (named B19) by merging three fragments JFM, U0P, and HWH. Through extensive all-atom molecular dynamics simulation and molecular docking, we found that B19 among all designed ones is most stable inside the Mpro's active site and the binding free energy of B19 is comparable to or even a little better than that of a native protein ligand processed by Mpro. Our promising results suggest that B19 and its derivatives can potentially be efficacious drug candidates for COVID-19.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.