Leupeptin, Microbial

Short Summary : Inhibitor of serine and cysteine proteases

Category : Proteases|Serine Protease

Purity : 0.98

CAS Number : 103476-89-7

Formula : C20H38N6O4.1/2H2SO4

Molecular Weight : 493.6

SMILE : O=C(C(C([H])([H])C(C([H])([H])[H])([H])C([H])([H])[H])([H])N([H])C(C([H])([H])[H])=O)N([H])C(C(N([H])C(C([H])=O)([H])C([H])([H])C([H])([H])C([H])([H])/N=C(N([H])[H])/N([H])[H])=O)([H])C([H])([H])C(C([H])([H])[H])([H])C([H])([H])[H]

Solubility : >24.7mg/mL in DMSO

Storage : Store at -20°C

Description : Leupeptin is a reversible inhibitor of protease with Ki values of 35 nM, 3.4 M, 6 nM and 72 nM for bovine trypsin, human plasmin, bovine spleen cathepsin B and recombinant human calpain, respectively [1, 2].
As a protease inhibitor, leupeptin was originally isolated from the Streptomyces species. It exerted poor membrane permeability due to its polar C-terminal. For calpain, leupeptin showed moderate potent activities with IC50 values of 0.211 M, 1.8 M and 0.938 M against the enzymes isolated from porcine erythrocyte, porcine kidney and human platelet, respectively. In cultured MRC-C cells, leupeptin suppressed the growth of human coronavirus strain 229E through inhibited the activity of trypsin. The mean IC50 value was 0.8 M [2, 3].
References:
1. Mehdi S. Cell-penetrating inhibitors of calpain. Trends in biochemical sciences, 1991, 16: 150-153.
2. Krauser J A, Powers J C. 6.1 BIOLOGICAL ROLES. Proteinase and Peptidase Inhibition: Recent Potential Targets for Drug Development, 2003: 144.
3. Appleyard G, Tisdale M. Inhibition of the growth of human coronavirus 229E by leupeptin. Journal of general virology, 1985, 66(2): 363-366.

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