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A reversible compeptitive protease inhibitor, which was shown to inhibit cathepsins B, H, L, and S, calpain and trypsin. Ac-LLR-CHO inhibits the trypsin-like activity of the proteasome endopeptidase complex. CAS Number (hemisulfate): 103476-89-7.

Leupeptin is a protease inhibitor that inhibits the activity of proteases in cells. It has been shown to inhibit transcriptional regulation and apoptosis pathway, as well as possessing anti-inflammatory properties. Leupeptin has been shown to have inhibitory properties against a variety of proteases, including group P2 metalloproteases, cathepsin D, and proteinase 3. This drug has also been shown to prevent neuronal death in experimental models by inhibiting cell lysis. Leupeptin binds to the active site of the enzyme by forming hydrogen bonds with conserved amino acid residues and steric interactions with nearby amino acid residues. The redox potentials of leupeptin are not known, but it is assumed that they are low enough for its antioxidant properties to be effective.

Leupeptin is an ion channel blocker that belongs to the group of protease inhibitors. It blocks the passage of ions across cell membranes by binding to the active site of a variety of enzymes in the membrane. Leupeptin is used as a research tool for studying protein interactions, and can be used for antibody production. Leupeptin is also useful in cell biology studies, because it inhibits the activation of many proteins involved in signal transduction and cell division.

Leupeptin is a naturally occurring protease inhibitor that has been synthetically produced for use as an experimental tool. Leupeptin inhibits the activity of basic proteins and enzymes by binding to them at the active site, preventing their access to substrate. This inhibition can be reversed with reducing agents (e.g., dithiothreitol). Leupeptin has been shown to inhibit neuronal death during anoxia in experimental models and has also been shown to have neurotrophic effects, which may be due to its ability to prevent protein aggregation.