PMC:7461420 / 32568-35550 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/7461420","sourcedb":"PMC","sourceid":"7461420","source_url":"https://www.ncbi.nlm.nih.gov/pmc/7461420","text":"2.4 Small‐molecules as cathepsin L inhibitors\nHuman cathepsin L is a cysteine endopeptidase and plays a key role for infection efficiency by activation of the S protein into a fusogenic state to escape the late endosomes. Targeting this protease with small molecules could interfere with virus‐cell entry and therefore be a possible intervention strategy for CoV infection. 114 Bates et al. identified MDL28170 (20; Figure 9) as an antiviral compound that specifically inhibited cathepsin‐L‐mediated substrate cleavage, with an IC50 value of 2.5 nM and EC50 value in the range of 100 nM. However, despite its potent inhibitory activity, no cytotoxicity data for 20 is currently available. 115\nFigure 9 Cathepsin L inhibitors with antiviral activity Diamond et al. reported CID 16725315 (21) and CID 23631927 (22; Figure 9) as viral entry inhibitors of SARS‐CoV in a cathepsin L inhibition assay. Compound 21 could block cathepsin L with an IC50 value of 6.9 nM, while 22 showed slightly weaker potency (IC50, 56 nM). Compound 22 was also found to inhibit Ebola virus infection (EC50, 193 nM) of human embryonic kidney 293T cells. This compound did not show any sign of toxicity to human aortic endothelial cells up to 100 µM. This data offers a new promising point for the treatment of SARS and Ebola virus infections. 116\nScreening of ~14 000 compounds in a cell‐based assay resulted in the identification of SSAA09E1 (23; Figure 9) as inhibitor of cathepsin L proteinase, with an IC50 value of 5.33 µM. In a pseudotype‐based assay in 293T cells, the EC50 value of 23 was around 6.4 µM, and no cytotoxicity was detected below 100 µM. 48\nPhenotypic screening approaches led to the identification of several viral entry inhibitors. This approach has the advantage of finding cellular‐active compounds, providing information on drug solubility and cell uptake. 117 On the other hand, it is limited in terms of capacity compared to in silico target‐based screening. Hsiang et al. identified emodin (24; Figure 9), the active component from Polygonum multiflorum and Rheum officinale, could block the interaction of S protein with ACE2, with an IC50 value of 10 µM and an EC50 value of 200 µM in an S protein‐pseudotyped retrovirus assay using Vero E6 cells. However, the mechanism of action of this compound still needs to be determined. 118 Sarafianos et al. 48 found that SSAA09E3 (25), a benzamide derivative of 24, could prevent virus‐cell membrane fusion in pseudotype‐based and antiviral‐based assays, with an EC50 value of 9.7 µM, but a CC50 value of 20 µM indicates additional unknown cellular targets.\nVE607 (26) was identified among 50 240 structurally diverse small molecules to specifically inhibit SARS‐CoV‐1 entry into cells using a phenotype‐based screening. Its EC50 value was reported at 3.0 µM and it inhibited SARS‐CoV‐1 plaque formation with an EC50 of 1.6 µM. 119 Cathepsin inhibitor E‐64‐D (27) blocked MERS‐CoV and SARS‐CoV‐1 infection as well. 120 , 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