ArticlePhytomedicine : international journal of phytotherapy and phytopharmacology2022
Discovery of Camellia sinensis catechins as SARS-CoV-2 3CL protease inhibitors through molecular docking, intra and extra cellular assays.
Article in Phytomedicine : international journal of phytotherapy and phytopharmacology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 30 citations in OpenAlex.
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- Diverse Structures of Tea Polyphenols from Rougui Wuyi Rock Tea and Their Potential as Inhibitor of 3C-like Protease.Molecules (Basel, Switzerland) · 2025Article
- Natural 7,8-secolignans fromJournal of traditional and complementary medicine · 2024Article
- In silico study unfolds inhibitory potential of epicatechin gallate against SARS-CoV-2 entry and replication within the host cell.Mechanobiology in medicine · 2023Article
- Review
- The Therapeutic Potential of Natural Dietary Flavonoids against SARS-CoV-2 Infection.Nutrients · 2023Review
- Identification of medicinal plant-based phytochemicals as a potential inhibitor for SARS-CoV-2 main protease (MComputers in biology and medicine · 2023Article
- Tea Plant (Nutrients · 2022Review
- Exploring new catechin derivatives as SARS-CoV-2 MComputers in biology and medicine · 2022Article
- The SARS-CoV-2 main protease (MMedComm · 2022Review
- SARS-CoV-2 neutralizing activity of polyphenols in a special green tea extract preparation.Phytomedicine : international journal of phytotherapy and phytopharmacology · 2022Article
- Single-cell sequencing of brain tissues reveal the central nervous system's susceptibility to SARS-CoV-2 and the drug.Frontiers in pharmacology · 2022Article
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Authors and funding
6 authors at 1 institution in 1 country.
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Abstract
background and purposePrevious studies suggest that major Camellia sinensis (tea) catechins can inhibit 3-chymotrypsin-like cysteine protease (3CLpro), inspiring us to study 3CLpro inhibition of the recently discovered catechins from tea by our group.
methodsAutodock was used to dock 3CLpro and 16 tea catechins. Further, a 3CLpro activity detection system was used to test their intra and extra cellular 3CLpro inhibitory activity. Surface plasmon resonance (SPR) was used to analyze the dissociation constant (K
resultsDocking data suggested that 3CLpro interacted with the selected 16 catechins with low binding energy through the key amino acid residues Thr24, Thr26, Asn142, Gly143, His163, and Gln189. The selected catechins other than zijuanin D (3) and (-)-8-(5''R)-N-ethyl-2-pyrrolidinone-3-O-cinnamoylepicatechin (11) can inhibit 3CLpro intracellularly. The extracellular 3CLpro IC
conclusionTogether, EC-C (1), etc-pyrrolidinone C and D (6), and GCG are strong 3CLpro inhibitors. Our results suggest that structural modification of catechins could be conducted by esterificating the 3-OH as well as changing the configuration of C-3, C-3''' or C-5''' to discover strong SARS-CoV-2 inhibitors.
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