ArticleScientific reports2020
Biochemical and biophysical characterization of the main protease, 3-chymotrypsin-like protease (3CLpro) from the novel coronavirus SARS-CoV 2.
Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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24 citing papers in PubMed, 46 citations in OpenAlex.
- Antiviral Activity of Pyrazolopyrimidine and Triazolopyrimidine Derivatives Against SARS-CoV-2 In Vitro: Identifying PZP25 as a Promising Scaffold.Pathogens (Basel, Switzerland) · 2026Article
- Structure-Guided Temporin L Analogs Development to Inhibit the Main Protease of SARS-CoV‑2.ACS medicinal chemistry letters · 2025Article
- Boosting immunity: synergistic antiviral effects of luteolin, vitamin C, magnesium and zinc against SARS-CoV-2 3CLpro.Bioscience reports · 2024Article
- 3-chymotrypsin-like protease in SARS-CoV-2.Bioscience reports · 2024Review
- Synthesis and biological evaluation of novel peptidomimetic inhibitors of the coronavirus 3C-like protease.European journal of medicinal chemistry · 2024Article
- Bayesian Inference Elucidates the Catalytic Competency of the SARS-CoV-2 Main Protease 3CLAnalytical chemistry · 2023Article
- Advances in research on 3C-like protease (3CLRSC medicinal chemistry · 2023Review
- The main protease 3CLpro of the SARS-CoV-2 virus: how to turn an enemy into a helper.Frontiers in bioengineering and biotechnology · 2023Article
- A hypothesis on designing strategy of effective RdRp inhibitors for the treatment of SARS-CoV-2.3 Biotech · 2023Review
- Surface cysteines could protect the SARS-CoV-2 main protease from oxidative damage.Journal of inorganic biochemistry · 2022Article
- Effect of pH on stability of dimer structure of the main protease of coronavirus-2.Biophysical chemistry · 2022Article
- Repurposing of anti-lung cancer drugs as multi-target inhibitors of SARS-CoV-2 proteins: An insight from molecular docking and MD-simulation study.Microbial pathogenesis · 2022Article
- Key dimer interface residues impact the catalytic activity of 3CLpro, the main protease of SARS-CoV-2.The Journal of biological chemistry · 2022Article
- A VSV-based assay quantifies coronavirus Mpro/3CLpro/Nsp5 main protease activity and chemical inhibition.Communications biology · 2022Article
- Molecular Interactions of Tannic Acid with Proteins Associated with SARS-CoV-2 Infectivity.International journal of molecular sciences · 2022Article
- Applying polypharmacology approach for drug repurposing for SARS-CoV2.Journal of chemical sciences (Bangalore, India) · 2022Article
- Design, synthesis andRSC advances · 2021Article
- Unveiling the Effect of Low pH on the SARS-CoV-2 Main Protease by Molecular Dynamics Simulations.Polymers · 2021Article
- Coronavirus disease 2019 (COVID-19): Biophysical and biochemical aspects of SARS-CoV-2 and general characteristics.Progress in biophysics and molecular biology · 2021Review
- Essentials in saline pharmacology for nasal or respiratory hygiene in times of COVID-19.European journal of clinical pharmacology · 2021Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Severe acute respiratory syndrome-coronavirus 2 (SARS-CoV-2) is responsible for the novel coronavirus disease 2019 (COVID-19). An appealing antiviral drug target is the coronavirus 3C-like protease (3CLpro) that is responsible for the processing of the viral polyproteins and liberation of functional proteins essential for the maturation and infectivity of the virus. In this study, multiple thermal analytical techniques have been implemented to acquire the thermodynamic parameters of 3CLpro at different buffer conditions. 3CLpro exhibited relatively high thermodynamic stabilities over a wide pH range; however, the protease was found to be less stable in the presence of salts. Divalent metal cations reduced the thermodynamic stability of 3CLpro more than monovalent cations; however, altering the ionic strength of the buffer solution did not alter the stability of 3CLpro. Furthermore, the most stable thermal kinetic stability of 3CLpro was recorded at pH 7.5, with the highest enthalpy of activation calculated from the slope of Eyring plot. The biochemical and biophysical properties of 3CLpro explored here may improve the solubility and stability of 3CLpro for optimum conditions for the setup of an enzymatic assay for the screening of inhibitors to be used as lead candidates in the discovery of drugs and design of antiviral therapeutics against COVID-19.
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