About: Design, synthesis and biological evaluation of a series of 5-chloropyridine ester-derived severe acute respiratory syndrome-coronavirus chymotrypsin-like protease inhibitors is described. Position of the carboxylate functionality is critical to potency. Inhibitor 10 with a 5-chloropyridinyl ester at position 4 of the indole ring is the most potent inhibitor with a SARS 3Clpro IC(50) value of 30 nM and antiviral EC(50) value of 6.9 μM. Molecular Docking studies have provided possible binding modes of these inhibitors. [Image: see text]   Goto Sponge  NotDistinct  Permalink

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  • Design, synthesis and biological evaluation of a series of 5-chloropyridine ester-derived severe acute respiratory syndrome-coronavirus chymotrypsin-like protease inhibitors is described. Position of the carboxylate functionality is critical to potency. Inhibitor 10 with a 5-chloropyridinyl ester at position 4 of the indole ring is the most potent inhibitor with a SARS 3Clpro IC(50) value of 30 nM and antiviral EC(50) value of 6.9 μM. Molecular Docking studies have provided possible binding modes of these inhibitors. [Image: see text]
subject
  • Esters
  • Protease inhibitors
  • Bat virome
  • Sarbecovirus
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