Anguizole

• CAT Number: I003567
• CAS Number: 442666-98-0
• Molecular Formula: C17H11ClF2N4O2S
• Molecular Weight: 408.81
• Purity: ≥95%
• Synonyms: 7-[chloro(difluoro)methyl]-5-(furan-2-yl)-N-(thiophen-2-ylmethyl)pyrazolo[1,5-a]pyrimidine-2-carboxamide
• Target: HCV Protease
• Solubility: 10 mM in DMSO
• Storage: Store at -20°C
• InChI: InChI=1S/C17H11ClF2N4O2S/c18-17(19,20)14-7-11(13-4-1-5-26-13)22-15-8-12(23-24(14)15)16(25)21-9-10-3-2-6-27-10/h1-8H,9H2,(H,21,25)
• InChIKey: GBNREAYNZPJROB-UHFFFAOYSA-N
• SMILES: O=C(C1=NN2C(C(F)(Cl)F)=CC(C3=CC=CO3)=NC2=C1)NCC4=CC=CS4

Anguizole is a small molecule inhibitor of HCV replication and alters NS4B/’s subcellular distribution.IC50 Value:Target: HCV

Reference

[1]. Bryson, Paul D. et al. A small molecule inhibits HCV replication and alters NS4B/’s subcellular distribution Antiviral Research (2010), 87(1), 1-8.
Abstract
Hepatitis C Virus (HCV) is a leading cause of liver disease and represents a significant public health challenge. Treatments for this disease are inadequate and improved antiviral therapies are necessary. Several such antivirals are in development, most of which target the well-characterized NS3 protease or the NS5B polymerase. In contrast, the nonstructural 4B (NS4B) protein, though essential for HCV RNA replication, has been the subject of few pharmacological studies. One of the functions ascribed to this protein is the ability to form intracellular membrane-associated foci (MAF), which are believed to be related to the sites of viral replication. Here, we report the identification of a small molecule that inhibits HCV replication and disrupts the organization of these MAF. Genetic analysis links the compound/’s mode of action to the NS4B gene product, and transient transfections of NS4B-GFP demonstrate that treatment with this compound can lead to the formation of novel elongated assemblies of NS4B….
[2]. Cho, Nam-Joon et al. Identification of a class of HCV inhibitors directed against the nonstructural protein NS4B. Science Translational Medicine (2010), 2(15), No pp. given.
Abstract
New classes of drugs are needed to combat hepatitis C virus (HCV), an important worldwide cause of liver disease. We describe an activity of a key domain, an amphipathic helix we termed 4BAH2, within a specific HCV nonstructural protein, NS4B. In addition to its proposed role in viral replication, we validate 4BAH2 as essential for HCV genome replication, and identify first generation small molecule inhibitors of 4BAH2 that specifically prevent HCV replication within cells. Detailed mechanistic studies reveal that the inhibitors target 4BAH2 function by either preventing 4BAH2 oligomerization or 4BAH2 membrane association. 4BAH2 inhibitors represent an exciting, additional class of compounds that has potential to effectively treat HCV.