| Weight | 426.562 g/mol |
|---|---|
| Formula | C20H38N6O4 |
| Hydrogen Acceptors | 5 |
| Hydrogen Donors | 5 |
| Aromatic Rings | 0 |
| Rotatable Bonds | 14 |
Leupeptin
103476-89-7, 24365-47-7, 55123-66-5
Score:
#53 in Molecular and cellular biology
,
#1674 in Biochemistry
,
#3753 in Biology
,
#4725 in Chemistry
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- Inhibition of the Lysosomal Pathway of Protein Degradation in Isolated Rat Hepatocytes by Ammonia, Methylamine, Chloroquine and Leupeptin (FEBS Journal, 1979)
- Leupeptin, a protease inhibitor, decreases protein degradation in normal and diseased muscles (Science, 1978)
- Inhibition of endosomal proteolytic activity by leupeptin blocks surface expression of MHC class II molecules and their conversion to SDS resistance alpha beta heterodimers in endosomes. (The EMBO Journal, 1992)
- Neurofilament accumulation induced in synapses by leupeptin (Science, 1983)
- Accumulation of autophagosomes after inhibition of hepatocytic protein degradation by vinblastine, leupeptin or a lysosomotropic amine (Experimental Cell Research, 1982)
- Inhibition of Tumorigenesis in Mouse Skin by Leupeptin, a Protease Inhibitor from Actinomycetes (Cancer Research, 1972)
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Predict GHS Hazards for Any Chemical in silico.
Including Acute Oral Tox, Skin Sensitization, Eye Irritation, Aquatic Tox, & more. -
SMILESCC(C)CC(C(=O)NC(CC(C)C)C(=O)NC(CCCN=C(N)N)C=O)NC(=O)C
-
InChIKeyGDBQQVLCIARPGH-UHFFFAOYSA-N
- Pubchem - Leupeptin
- Wikipedia - leupeptin
Leupeptin, also known as N-acetyl-L-leucyl-L-leucyl-L-argininal, is a naturally occurring protease inhibitor that can inhibit cysteine, serine and threonine peptidases. It is often used during in vitro experiments when a specific enzymatic reaction is being studied. When cells are lysed for these studies, proteases, many of which are contained within lysosomes, are released.
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Synthesis
urea
+
Reactant
(Imine formation from aldehyde)
Reactant
+
Oxalyl chloride
(Swern oxidation)
ACETYL CHLORIDE
+
Reactant
(Schotten-Baumann amide from acid)
acetamide
+
Reactant
(Alkylation of primary amines)
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