ALLM (136632-32-1) is a cell-permeable, peptide aldehyde inhibitor of calpain (calpain I, Ki= 120 nM, calpain II, Ki= 230 nM) and other neutral cysteine proteases. Potent inhibitor of cathepsin L (Ki=0.6 nM) and cathepsin B (Ki=100 nM).1Weak inhibitor of the chymotrypsin-like activity of the proteasome.2Cell permeable.
ALLM (Calpain Inhibitor) is a cell-permeable, peptide aldehyde inhibitor of calpain I and calpain II. ALLM acts as a very potent inhibitor of cathepsin L and the strongest inhibitor of cathepsin B amongst the peptide aldehydes. This compound inhibits the processing of malaria aspartic hemoglobinases plasmepsins I and IIin vitro. ALLM also inhibits other neutral cysteine proteases, and activation-induced programmed cell death. It restores defective immune responses in HIV+ donors. ALLM blocks nitric oxide production by activated macrophages by interfering with transcription of the inducible nitric oxide synthase gene. ALLM also acts as a weak inhibitor of proteasome.
Calpain inhibitor II is a cell-permeable peptide that restricts the activity of calpain, cathepsin L and cathepsin B. Calpain inhibitor II also prevents the methylmercury-induced cell death of cultured rat cerebellar neurons.
ChEBI: (2S)-2-acetamido-4-methyl-N-[4-methyl-1-[[4-(methylthio)-1-oxobutan-2-yl]amino]-1-oxopentan-2-yl]pentanamide is a peptide.
[1] T SASAKI. Inhibitory effect of di- and tripeptidyl aldehydes on calpains and cathepsins.[J]. Journal of enzyme inhibition, 1990, 3 3: 195-201. DOI:
10.3109/14756369009035837[2] ALEXANDER VINITSKY. Inhibition of the chymotrypsin-like activity of the pituitary multicatalytic proteinase complex[J]. Biochemistry Biochemistry, 1992, 31 39: 9421-9428. DOI:
10.1021/bi00154a014
