 | |
| Names | |
|---|---|
| IUPAC name N-Acetyl-leucyl-N-{[5-[(diaminomethylidene)amino]-1-oxopentan-2-yl}-leucinamide[citation needed] | |
| Identifiers | |
3D model (JSmol) | |
| ChEBI | |
| ChemSpider |
|
| ECHA InfoCard | 100.212.237 |
| UNII | |
| |
| |
| Properties | |
| C20H38N6O4 | |
| Molar mass | 426.562 g·mol−1 |
| Related compounds | |
Related alkanamides | Gusperimus |
Related compounds | Synthalin |
Except where otherwise noted, data are given for materials in theirstandard state (at 25 °C [77 °F], 100 kPa). | |
Leupeptin, also known asN-acetyl-L-leucyl-L-leucyl-L-argininal, is a naturally occurringprotease inhibitor that can inhibit cysteine, serine and threonine peptidases.
It is often used duringin vitro experiments when a specific enzymatic reaction is being studied. When cells are lysed for these studies,proteases, many of which are contained withinlysosomes, are released. These proteases, if freely present in the lysate, would destroy any products from the reaction being studied, and make the experiment uninterpretable. For example, leupeptin could be used in acalpain extraction to keep calpain from being hydrolyzed by specific proteases. The suggested concentration is 1-10 μM (0.5-5 μg/ml).
Leupeptin is an organic compound produced byactinomycetes, which inhibitsserine,cysteine andthreonine proteases. Leupeptin inhibits serine proteinases (trypsin (Ki=3.5 nM),plasmin (Ki= 3.4 nM), porcinekallikrein), and cysteine proteinases (papain,cathepsin B (Ki = 4.1 nM),endoproteinase Lys-C). It does not inhibit α-chymotrypsin orthrombin. Leupeptin is a competitive transition state inhibitor and its inhibition may be relieved by an excess of substrate.
Leupeptin is soluble in water (stable for 1 week at 4 °C and 1 month at −20 °C), ethanol, acetic acid and DMF.
It can be given topically for middle and inner ear infections.[1]
