122520-85-8

Basic information

• Product Name: AG 99
• Synonyms: TYRPHOSTIN AG 99;TYRPHOSTIN B40;TYRPHOSTIN 46;TYRPHOSTIN A46;3,4-DIHYDROXY-ALPHA-CYANOCINNAMIDE;ALPHA-CYANO-(3,4-DIHYDROXY)CINNAMIDE;AG 99;(E)-2-CYANO-3-(3,4-DIHYDROXYPHENYL)-2-PROPENAMIDE
• CAS NO: 122520-85-8
• Molecular Formula: C₁₀H₈N₂O₃
• Molecular Weight: 204.18
• Product Categories: ALCOHOL;Intracellular Signaling
• Mol File: 122520-85-8.mol
• Article Data: 9

Chemical Properties

• Melting Point: 247 °C
• Boiling Point: 544.4°Cat760mmHg
• Flash Point: 283°C
• Appearance: /
• Density: 1.482g/cm³
• Storage Temp.: Desiccate at +4°C
• Solubility: Soluble in DMSO
• PKA: 8.81±0.10(Predicted)
• CAS DataBase Reference: AG 99(CAS DataBase Reference)
• NIST Chemistry Reference: AG 99(122520-85-8)
• EPA Substance Registry System: AG 99(122520-85-8)

Safety Data

• Hazardous Substances Data: 122520-85-8(Hazardous Substances Data)

Usage

Biological Activity

Epidermal growth factor receptor (EGFR) kinase inhibitor (IC 50 = 10 μ M) that is selective over insulin receptor kinase. Blocks tyrosine phosphorylation of p145 met and promotes cell death of normal and cancer cells via activation of caspase-like proteases in vitro .

references

[1]. gazit a, osherov n, gilon c, et al. tyrphostins. 6. dimeric benzylidenemalononitrile tyrophostins: potent inhibitors of egf receptor tyrosine kinase in vitro. j med chem, 1996, 39(25): 4905-4911.[2]. yamamoto n, mammadova g, song rx, et al. tyrosine phosphorylation of p145met mediated by egfr and src is required for serum-independent survival of human bladder carcinoma cells. j cell sci, 2006, 119(pt 22): 4623-4633.

Upstream product

• 139-85-5 3,4-dihydroxybenzaldehyde 
• 105-56-6 ethyl 2-cyanoacetate 
• 7664-93-9 sulfuric acid 
• 118409-57-7 α-cyano-(3,4-dihydroxy)cinnamonitrile 
• 107-91-5 cyanoacetic acid amide 

Relevant articles and documents

Development of the First Two-Pore Domain Potassium Channel TWIK-Related K+ Channel 1-Selective Agonist Possessing in Vivo Antinociceptive Activity

The TWIK-related K+ channel, TREK-1, has recently emerged as an attractive therapeutic target for the development of a novel class of analgesic drugs, suggesting that activation of TREK-1 could result in pain inhibition. Here, we report the synthesis of a series of substituted acrylic acids (1-54) based on our previous work with caffeate esters. The analogues were evaluated for their ability to modulate TREK-1 channel by electrophysiology and for their in vivo antinociceptive activity (acetic acid-induced writhing and hot plate assays), leading to the identification of a series of novel molecules able to activate TREK-1 and displaying potent antinociceptive activity in vivo. Furyl analogue 36 is the most promising of the series.

Arylcyanoacrylamides as inhibitors of the Dengue and West Nile virus proteases

The 3-aryl-2-cyanoacrylamide scaffold was designed as core pharmacophore for inhibitors of the Dengue and West Nile virus serine proteases (NS2B-NS3). A total of 86 analogs was prepared to study the structure-activity relationships in detail. Thereby, it turned out that the electron density of the aryl moiety and the central double bond have a crucial influence on the activity of the compounds, whereas the influence of substituents of the amide residue is less relevant. The para-hydroxy substituted analog was found to be the most potent inhibitor in this series with a Ki-value of 35.7 μM at the Dengue and 44.6 μM at the West Nile virus protease. The aprotinin competition assay demonstrates a direct interaction of the inhibitor molecule with active centre of the Dengue virus protease. The target selectivity was studied in a counterscreen with thrombin and found to be 2.8:1 in favor of DEN protease and 2.3:1 in favor of WNV protease, respectively.

Bicyclic compounds as ring-constrained inhibitors of protein-tyrosine kinase p56(lck)

A study was undertaken to prepare inhibitors of the lymphocyte protein- tyrosine kinase p56(lck). Using the known p56(lck) inhibitor 3,4-dihydroxy- α-cyanocinnamamide (4) as a lead compound, bicyclic analogues were designed as conformationally constrained