Synonym: N-(Nα-Carbonyl-Cpd-X-Phe-al)-Phe (Cpd = capreomycidine) (capreomycidine = [S,S]-α-(2-Iminohexahydro-4-pyrimidyl)glycine)
|Related Categories||A to C, Apoptosis Enzymes, Application Index, Bioactive Small Molecules, Biochemicals and Reagents,|
|solubility||DMSO: soluble10 mM (Stock solutions stable for months at −20 °C.)|
Chymostatin is a strong inhibitor of many proteases, including chymotrypsin, papain, chymotrypsin-like serine proteinases, chymases, and lysosomal cysteine proteinases such as cathepsins A,B,C, B, H, and L. It weakly inhibits human leucocyte elastase. It is effective at a final concentration of 100 to 200 μg/ml (10 to 100 μM). Chymostatin is often included in protease inhibitor cocktails used with plant extracts.
Inhibits the lysosomal proteinase cathepsin B, and the soluble Ca2+-activated proteinase.1 Many young plant tissues express a chomostatin-sensitive serine protease.2
A mixture of A (major), B and C components. A: X=Leu; B: X=Val; C: X=Ile
chymostatin A MW = 607.7
chymostatin B MW = 593.7
chymostatin C MW = 607.7
Solubility testing in glacial acetic acid at 10 mg/ml yields a clear solution, which is usually colorless, but can be yellow in appearance. It is reportedly also soluble in DMSO; only slightly soluble in water and short-chain alcohols; insoluble in ethyl acetate, butyl acetate, ether, hexane, and petroleum ether. Stock solutions (10 mM) can be prepared in DMSO and are stable for months at -20 °C. Stock solutions can also be made in 0.1 M HCl. Dilute solutions (10-100 μM) are only stable for several hours, due to oxidation of the terminal aldehyde.
Chymostatin has been used in a study that determined that molecular calculations are useful for evaluating the interactions between ligands, including inhibitors and homologous enzymes, in docking models. Chymostatin has also been used in a study to investigate the norovirus protease as an attractive target for antiviral drug development.
Certificate of Analysis
Certificate of Origin
Beynon, R.J. and Bond, J.S., ed. Proteolytic Enzymes: A Practical Approach New York, NY , (1989), 207,243
Levy, M.R. and Chou, S.C. Biochim. Biophys. Acta 334, 423, (1974)
Comparative analysis of binding energy of chymostatin with human cathepsin A and its homologous proteins by molecular orbital calculation Yoshida, T., et al. J. Chem. Inf. Model. 46, 2093-103, (2012)
ACE-dependent and chymase-dependent angiotensin II generation in normal and glucose-stimulated human mesangial cells. Cristovam PC, Arnoni CP, de Andrade MC, et al. Exp. Biol. Med. (Maywood.) 233(8), 1035-43, (2008)
Contractility of placental vascular smooth muscle cells in response to stimuli produced by the placenta: roles of ACE vs. non-ACE and AT1 vs. AT2 in placental vessel cells. Benoit C Placenta 29(6), 503-9, (2008)
Chymostatin can combine with pepstatin to eliminate extracellular protease activity in cultures of Aspergillus niger NRRL-3. Ahamed A, Singh A, and Ward OP J. Ind. Microbiol. Biotechnol. 34(2), 165-9, (2007)
Determination of the cytotoxic effect of Clostridium histolyticum culture supernatant on HeLa cells in the presence of protease inhibitors. Jóźwiak J, Komar A, Jankowska E, et al. FEMS Immunol. Med. Microbiol. 45(2), 137-42, (2005)
Cathepsin G induces cell aggregation of human breast cancer MCF-7 cells via a 2-step mechanism: catalytic site-independent binding to the cell surface and enzymatic activity-dependent induction of the cell aggregation. Morimoto-Kamata R, Mizoguchi S, Ichisugi T, et al. Mediators Inflamm. 2012, 456462, (2012)
A new look at the pathogenesis of the meconium aspiration syndrome: a role for fetal pancreatic proteolytic enzymes in epithelial cell detachment. Ivanov VA, Gewolb IH, and Uhal BD Pediatr. Res. 68(3), 221-4, (2010)
Comparative analysis of binding energy of chymostatin with human cathepsin A and its homologous proteins by molecular orbital calculation. Yoshida T, Lepp Z, Kadota Y, et al. J. Chem. Inf. Model. 46(5), 2093-103, (2006)
Cordysobin, a novel alkaline serine protease with HIV-1 reverse transcriptase inhibitory activity from the medicinal mushroom Cordyceps sobolifera Wang, S., et al. J. Biosci. Bioeng. 113(1), 42-7, (2011)
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