z-lvg-chn2

The diazomethyl ketone Z-LVG-CHN2 mimics part of the human cysteine proteinase-binding center, has been shown to be an irreversible inhibitor of this proteinase. The compound was also tested for antiviral activity against herpes simplex virus type 1 (HSV) and found to block the HSV replication. Irreversible inhibitor of streptopain.

Z-L(D-Val)G-CHN2, an isoform of Z-LVG-CHN2, serves as a cell-permeable and irreversible inhibitor of cysteine proteinase. This tripeptide derivative emulates a segment of the human cysteine proteinase-binding center and demonstrates selective antiviral activity, inhibiting herpes simplex virus (HSV) yet exhibiting negligible impact on poliovirus replication. Notably, Z-LVG-CHN2 effectively impedes SARS-CoV-2 replication with an EC50 value of 190 nM by targeting the SARS-CoV-2 3CL protease [3].