TC-S 7010

• CAT Number: I000575
• CAS Number: 1158838-45-9
• Molecular Formula: C₃₁H₃₁ClFN₇O₂
• Molecular Weight: 588.07
• Purity: ≥95%
• Synonyms: N-(2-chlorophenyl)-4-[[2-[4-[2-(4-ethylpiperazin-1-yl)-2-oxoethyl]anilino]-5-fluoropyrimidin-4-yl]amino]benzamide
• Target: Aurora Kinase
• Solubility: DMSO ≥115mg/mL Water <1.2mg/mL Ethanol <1.2mg/mL
• Storage: 3 years -20C powder
• IC50: 3.4 nM
• InChI: InChI=1S/C31H31ClFN7O2/c1-2-39-15-17-40(18-16-39)28(41)19-21-7-11-24(12-8-21)36-31-34-20-26(33)29(38-31)35-23-13-9-22(10-14-23)30(42)37-27-6-4-3-5-25(27)32/h3-14,20H,2,15-19H2,1H3,(H,37,42)(H2,34,35,36,38)
• InChIKey: AKSIZPIFQAYJGF-UHFFFAOYSA-N
• SMILES: CCN1CCN(CC1)C(=O)CC2=CC=C(C=C2)NC3=NC=C(C(=N3)NC4=CC=C(C=C4)C(=O)NC5=CC=CC=C5Cl)F

TC-S 7010（Cat No.:I000575）is a potent and selective inhibitor of the protein arginine methyltransferase 5 (PRMT5), an enzyme implicated in various cancers and disease processes. By inhibiting PRMT5, TC-S 7010 disrupts the methylation of arginine residues on target proteins, affecting gene expression, cell proliferation, and survival pathways in cancer cells. This compound has shown promise in preclinical studies, particularly in hematological malignancies and solid tumors, where it may enhance the efficacy of other treatments. Its specificity for PRMT5 makes TC-S 7010 a valuable tool for studying arginine methylation in cancer biology and potential therapeutic applications.

Reference

[1]. Aliagas-Martin I, Burdick D, Corson L, Dotson J, Drummond J, Fields C, Huang OW, Hunsaker T, Kleinheinz T, Krueger E, Liang J, Moffat J, Phillips G, Pulk R, Rawson TE, Ultsch M, Walker L, Wiesmann C, Zhang B, Zhu BY, Cochran AG.A class of 2,4-bisanilinopyrimidine Aurora A inhibitors with unusually high selectivity against Aurora B.J Med Chem. 2009 May 28;52(10):3300-7.
Abstract
The two major Aurora kinases carry out critical functions at distinct mitotic stages. Selective inhibitors of these kinases, as well as pan-Aurora inhibitors, show antitumor efficacy and are now under clinical investigation. However, the ATP-binding sites of Aurora A and Aurora B are virtually identical, and the structural basis for selective inhibition has therefore not been clear. We report here a class of bisanilinopyrimidine Aurora A inhibitors with excellent selectivity for Aurora A over Aurora B, both in enzymatic assays and in cellular phenotypic assays. Crystal structures of two of the inhibitors in complex with Aurora A implicate a single amino acid difference in Aurora B as responsible for poor inhibitory activity against this enzyme. Mutation of this residue in Aurora B (E161T) or Aurora A (T217E) is sufficient to swap the inhibition profile, suggesting that this difference might be exploited more generally to achieve high selectivity for Aurora A.