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Cysteine Protease inhibitor

CAS# 921625-62-9

Cysteine Protease inhibitor

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Chemical structure

Cysteine Protease inhibitor

3D structure

Chemical Properties of Cysteine Protease inhibitor

Cas No. 921625-62-9 SDF Download SDF
PubChem ID 12000657 Appearance Powder
Formula C18H14N4O M.Wt 302.33
Type of Compound N/A Storage Desiccate at -20°C
Synonyms 2-Pyrimidinecarbonitrile, 4-[[4'-(aminomethyl)[1,1'-biphenyl]-3-yl]oxy]-
Solubility DMSO : 50 mg/mL (165.38 mM; Need ultrasonic)
Chemical Name 4-[3-[4-(aminomethyl)phenyl]phenoxy]pyrimidine-2-carbonitrile
SMILES C1=CC(=CC(=C1)OC2=NC(=NC=C2)C#N)C3=CC=C(C=C3)CN
Standard InChIKey RMVQVAZRAZGSTH-UHFFFAOYSA-N
Standard InChI InChI=1S/C18H14N4O/c19-11-13-4-6-14(7-5-13)15-2-1-3-16(10-15)23-18-8-9-21-17(12-20)22-18/h1-10H,11,19H2
General tips For obtaining a higher solubility , please warm the tube at 37 ℃ and shake it in the ultrasonic bath for a while.Stock solution can be stored below -20℃ for several months.
We recommend that you prepare and use the solution on the same day. However, if the test schedule requires, the stock solutions can be prepared in advance, and the stock solution must be sealed and stored below -20℃. In general, the stock solution can be kept for several months.
Before use, we recommend that you leave the vial at room temperature for at least an hour before opening it.
About Packaging 1. The packaging of the product may be reversed during transportation, cause the high purity compounds to adhere to the neck or cap of the vial.Take the vail out of its packaging and shake gently until the compounds fall to the bottom of the vial.
2. For liquid products, please centrifuge at 500xg to gather the liquid to the bottom of the vial.
3. Try to avoid loss or contamination during the experiment.
Shipping Condition Packaging according to customer requirements(5mg, 10mg, 20mg and more). Ship via FedEx, DHL, UPS, EMS or other couriers with RT, or blue ice upon request.

Cysteine Protease inhibitor Dilution Calculator

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Cysteine Protease inhibitor Molarity Calculator

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Preparing Stock Solutions of Cysteine Protease inhibitor

1 mg 5 mg 10 mg 20 mg 25 mg
1 mM 3.3076 mL 16.5382 mL 33.0764 mL 66.1529 mL 82.6911 mL
5 mM 0.6615 mL 3.3076 mL 6.6153 mL 13.2306 mL 16.5382 mL
10 mM 0.3308 mL 1.6538 mL 3.3076 mL 6.6153 mL 8.2691 mL
50 mM 0.0662 mL 0.3308 mL 0.6615 mL 1.3231 mL 1.6538 mL
100 mM 0.0331 mL 0.1654 mL 0.3308 mL 0.6615 mL 0.8269 mL
* Note: If you are in the process of experiment, it's necessary to make the dilution ratios of the samples. The dilution data above is only for reference. Normally, it's can get a better solubility within lower of Concentrations.

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Background on Cysteine Protease inhibitor

Cysteine Protease inhibitor is an inhibitor of cysteine protease. IC50 & Target: Cysteine Protease

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References on Cysteine Protease inhibitor

Odanacatib, a Cathepsin K Cysteine Protease Inhibitor, Kills Hookworm In Vivo.[Pubmed:27384569]

Pharmaceuticals (Basel). 2016 Jul 4;9(3). pii: ph9030039.

Hookworm infection is chief among soil-transmitted helminthiases (STHs) for the chronic morbidly inflicted. Deworming via mass drug administration (MDA) programs most often employs single doses of benzimidazole drugs to which resistance is a constant threat. To discover new drugs, we employ a hamster model of hookworm infection with Ancylostoma ceylanicum and use albendazole (ABZ; 10 mg/kg orally) as the gold standard therapy. We previously showed that a single oral 100 mg/kg dose of the cathepsin cysteine protease (CP) inhibitor, K11777, offers near cure of infection that is associated with a 95% reduction in the parasite's resident CP activity. We confirm these findings here and demonstrate that odanacatib (ODN), Merck's cathepsin K inhibitor and post-clinical Phase III drug candidate for treatment of osteoporosis, decreases worm burden by 73% at the same dose with a 51% reduction in the parasite's CP activity. Unlike K11777, ODN is a modest inhibitor of both mammalian cathepsin B and the predominant cathepsin B-like activity measureable in hookworm extracts. ODN's somewhat unexpected efficacy, therefore, may be due to its excellent pharmacokinetic (PK) profile which allows for sustained plasma exposure and, possibly, sufficient perturbation of hookworm cathepsin B activity to be detrimental to survival. Accordingly, identifying a CP inhibitor(s) that combines the inhibition potency of K11777 and the PK attributes of ODN could lead to a drug that is effective at a lower dose. Achieving this would potentially provide an alternative or back-up to the current anti-hookworm drug, albendazole.

Loss of second and sixth conserved cysteine residues from trypsin inhibitor-like cysteine-rich domain-type protease inhibitors in Bombyx mori may induce activity against microbial proteases.[Pubmed:27677962]

Peptides. 2016 Dec;86:13-23.

Previous studies have indicated that most trypsin inhibitor-like cysteine-rich domain (TIL)-type protease inhibitors, which contain a single TIL domain with ten conserved cysteines, inhibit cathepsin, trypsin, chymotrypsin, or elastase. Our recent findings suggest that Cys(2nd) and Cys(6th) were lost from the TIL domain of the fungal-resistance factors in Bombyx mori, BmSPI38 and BmSPI39, which inhibit microbial proteases and the germination of Beauveria bassiana conidia. To reveal the significance of these two missing cysteines in relation to the structure and function of TIL-type protease inhibitors in B. mori, cysteines were introduced at these two positions (D36 and L56 in BmSPI38, D38 and L58 in BmSPI39) by site-directed mutagenesis. The homology structure model of TIL domain of the wild-type and mutated form of BmSPI39 showed that two cysteine mutations may cause incorrect disulfide bond formation of B. mori TIL-type protease inhibitors. The results of Far-UV circular dichroism (CD) spectra indicated that both the wild-type and mutated form of BmSPI39 harbored predominantly random coil structures, and had slightly different secondary structure compositions. SDS-PAGE and Western blotting analysis showed that cysteine mutations affected the multimerization states and electrophoretic mobility of BmSPI38 and BmSPI39. Activity staining and protease inhibition assays showed that the introduction of cysteine mutations dramaticly reduced the activity of inhibitors against microbial proteases, such as subtilisin A from Bacillus licheniformis, protease K from Engyodontium album, protease from Aspergillus melleus. We also systematically analyzed the key residue sites, which may greatly influence the specificity and potency of TIL-type protease inhibitors. We found that the two missing cysteines in B. mori TIL-type protease inhibitors might be crucial for their inhibitory activities against microbial proteases. The genetic engineering of TIL-type protease inhibitors may be applied in both health care and agricultural industries, and could lead to new methods for breeding fungus-resistant transgenic crops and antifungal transgenic silkworm strains.

Heterologous expression of the plant cysteine protease bromelain and its inhibitor in Pichia pastoris.[Pubmed:27860461]

Biotechnol Prog. 2017 Jan;33(1):54-65.

Expression of proteases in heterologous hosts remains an ambitious challenge due to severe problems associated with digestion of host proteins. On the other hand, proteases are broadly used in industrial applications and resemble promising drug candidates. Bromelain is an herbal drug that is medicinally used for treatment of oedematous swellings and inflammatory conditions and consists in large part of proteolytic enzymes. Even though various experiments underline the requirement of active cysteine proteases for biological activity, so far no investigation succeeded to clearly clarify the pharmacological mode of action of bromelain. The potential role of proteases themselves and other molecules of this multi-component extract currently remain largely unknown or ill defined. Here, we set out to express several bromelain cysteine proteases as well as a bromelain inhibitor molecule in order to gain defined molecular entities for subsequent studies. After cloning the genes from its natural source Ananas comosus (pineapple plant) into Pichia pastoris and subsequent fermentation and purification, we obtained active protease and inhibitor molecules which were subsequently biochemically characterized. Employing purified bromelain fractions paves the way for further elucidation of pharmacological activities of this natural product. (c) 2016 American Institute of Chemical Engineers Biotechnol. Prog., 33:54-65, 2017.

Cysteine protease inhibitor of Schistosoma japonicum - A parasite-derived negative immunoregulatory factor.[Pubmed:28066871]

Parasitol Res. 2017 Mar;116(3):901-908.

Studies have shown that Cysteine Protease inhibitors from some parasites have immunosuppressive effects on the host. We previously have cloned a novel Cysteine Protease inhibitor from Schistosoma japonicum and purified its recombinant version (protein named rSj-C). Its possible inhibitory effect on the host immune response has not been described.This study shows that rSj-C inhibits lysosomal cysteine protease of murine dendritic cells (DCs). After DCs were incubated with rSj-C and then with soluble adult worm antigen (AWA) of S. japonicum, the mean fluorescence intensity of MHC class II antigens on the surface of DCs decreased significantly by flow cytometry. These results indirectly proved that rSj-C can suppress exogenous-antigen presentation by DCs. The flow cytometric assay revealed that in comparison with control groups, the proportion of CD4(+)CD25(+)Foxp3(+) T cells among CD4(+)CD25(+) T cells of Schistosom-infected mice increased significantly 8 weeks after the infected mice were injected with rSj-C (p < 0.05). Additionally, the expression levels of cytokines IL-4 and TGF-beta produced by T cells increased significantly as compared with these levels in the normal group (p < 0.05). These results clearly show that the Cysteine Protease inhibitor from S. japonicum is a new parasite-derived immunosuppressive factor.

Description

Cysteine Protease inhibitor is an inhibitor of cysteine protease.

Keywords:

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