62004-35-7

Basic information

• Product Name: LFM-A13
• Synonyms: LFM-A13;2-CYANO-N-(2,5-DIBROMOPHENYL)-3-HYDROXY-2-BUTENAMIDE;ALPHA-CYANO-BETA-HYDROXY-BETA-METHYL-N-(2,5-DIBROMOPHENYL)PROPENAMIDE;2-Cyano-N-(2,5-dibromophenyl)-3-hydroxy-2-buteneamide;2-Cyano-3-hydroxy-but-2-enoic acid (2,5-dibromo-phenyl)-amide
• CAS NO: 62004-35-7
• Molecular Formula: C11H8Br2N2O2
• Molecular Weight: 360
• Product Categories: Protein Kinase;Growth Factors and Cytokines;Intracellular Signaling
• Mol File: 62004-35-7.mol
• Article Data: 7

Chemical Properties

• Boiling Point: 487.9°C at 760 mmHg
• Flash Point: 248.9°C
• Appearance: white/powder
• Density: 1.909g/cm³
• Vapor Pressure: 2.47E-10mmHg at 25°C
• Refractive Index: 1.677
• Storage Temp.: −20°C
• Solubility: DMSO: 15 mg/mL
• CAS DataBase Reference: LFM-A13(CAS DataBase Reference)
• NIST Chemistry Reference: LFM-A13(62004-35-7)
• EPA Substance Registry System: LFM-A13(62004-35-7)

Safety Data

• Hazard Codes: Xn
• Statements: 20/21/22
• Safety Statements: 36/37
• WGK Germany: 3
• Hazardous Substances Data: 62004-35-7(Hazardous Substances Data)

Usage

Uses

LFM-A13 is a novel anti-leukemic agent targeting Bruton''s tyrosine kinase (BTK). LFM-A13 is a BTK inhibitor.

Biological Activity

Potent and selective inhibitor of Bruton's tyrosine kinase (BTK). Inhibits recombinant BTK with an IC 50 value of 2.5 μ M and has no activity on other protein kinases ( including JAK1, JAK3, HCK, EGFR kinase and insulin receptor kinase) at concentrations of up to 278 μ M.

InChI:InChI=1/C11H8Br2N2O2/c1-6(16)8(5-14)11(17)15-10-4-7(12)2-3-9(10)13/h2-4,16H,1H3,(H,15,17)/b8-6-

Upstream product

• 63034-99-1 N-(2,5-dibromophenyl)-2-cyanoacetamide 
• 75-36-5 acetyl chloride 
• 3638-73-1 2,5-dibromoaniline 
• 108-24-7 acetic anhydride 

Relevant articles and documents

ATP competitive inhibitors of d-alanine-d-alanine ligase based on protein kinase inhibitor scaffolds

d-Alanine-d-alanine ligase (DDl) is an essential enzyme in bacterial cell wall biosynthesis and an important target for developing new antibiotics. Here, we describe a new approach to identify new inhibitor scaffolds for DDl based on similarity in the ATP

Structural influence on the intermolecular/intramolecular hydrogen bonding in solid state of substituted leflunomides: Evidence by X-ray crystal structure

We report the results of an X-ray crystal structure study of nine substituted leflunomide metabolite analogs (LFM). Comparison of the hydrogen bonding characteristics exhibited by these structurally distinct LFM analogs was especially informative about the inter- and intra-molecular hydrogen bonding patterns that exist in the crystal structure of individual compounds. All compounds had the strong intramolecular hydrogen bonds. In addition, with the exception of the 2,5-difluorophenyl substituted LFM analog, all other compounds formed inter- or intra-molecular hydrogen bonds with the halogen atom and the NH group. However, we found that the presence of a fluorine atom at the 2-position on the phenyl ring of the 2,5-difluoro and 2-fluoro derivatives resulted in only one intramolecular hydrogen bond in the structural framework. Conversely, the 3,5-difluoro substituted LFM analog had an intramolecular hydrogen bond common to the other halide substituted derivatives. The anomaly exhibited by the 2,5-difluoro and the 2-fluoro substituted compounds may be owing to the smaller size of fluorine atom in comparison with the chlorine and bromine atoms in the structures of the other analogs. The presence of a fluorine at the 2-position of the phenyl ring may disrupt the intermolecular hydrogen bonding that was observed for the other derivatives due to differences in the crystal packing for these molecules.

Inhibitors of the EGF-receptor tyrosine kinase and methods for their use

Novel compounds and pharmaceutical compositions useful as EGFR tyrosine kinase inhibitors. Methods of the invention include administration of the EGFR TK inhibitors to treat diseases characterized by enhanced expression of EGF, including cancers, particularly breast cancer. Additionally, a homology model representing the structure of EGFR kinase domain is provided, which model is useful for the rationally design and screening of compounds predicted to bind favorably to EGFR and to inhibit EGFR TK.