5515-10-6

Upstream product

• 100-07-2 4-methoxy-benzoyl chloride 
• 109-77-3 malononitrile 
• 100-09-4 4-methoxybenzoic acid 

Downstream Products

• 91135-52-3 3-Imino-2-<4-methoxy-benzoyl>-acrylonitril 
• 111479-94-8 β-benzoyloxy-α-cyano-p-methoxycinnamonitrile 
• 5515-13-9 2-Cyan-3-methoxy-3-<4-methoxy-phenyl>-acrylonitril 

Relevant academic research and scientific papers

Studies on the ATP Binding Site of Fyn Kinase for the Identification of New Inhibitors and Their Evaluation as Potential Agents against Tauopathies and Tumors

Fyn is a member of the Src-family of nonreceptor protein-tyrosine kinases. Its abnormal activity has been shown to be related to various human cancers as well as to severe pathologies, such as Alzheimer's and Parkinson's diseases. Herein, a structure-based drug design protocol was employed aimed at identifying novel Fyn inhibitors. Two hits from commercial sources (1, 2) were found active against Fyn with Ki of about 2 μM, while derivative 4a, derived from our internal library, showed a Ki of 0.9 μM. A hit-to-lead optimization effort was then initiated on derivative 4a to improve its potency. Slightly modifications rapidly determine an increase in the binding affinity, with the best inhibitors 4c and 4d having Kis of 70 and 95 nM, respectively. Both compounds were found able to inhibit the phosphorylation of the protein Tau in an Alzheimer's model cell line and showed antiproliferative activities against different cancer cell lines. (Chemical Equation Presented).

Pyrrole derivatives as potent inhibitors of lymphocyte-specific kinase: Structure, synthesis, and SAR

We have described the synthesis, enzyme inhibitory activity, structure-activity relationships, and proposed binding mode of a novel series of pyrrole derivatives as lymphocyte-specific kinase (Lck) inhibitors. The most potent analogs exhibited good enzyme inhibitory activity (IC50s 10 nM) for Lck kinase inhibition.

Tyrphostins I: Synthesis and Biological Activity of Protein Tyrosine Kinase Inhibitors

A novel class of low molecular weight proteine kinase inhibitors is described.These compounds consitute a systematic series of molecules with a progressive increase in affinity toward the substrate site of the EGF receptor kinase domain.These competitive inhibitors also effectively block the EGF-dependent autophosphorylation of the receptor.The potent EGF receptor kinase blockers examined were found to competitively inhibit the homologous insulin receptor kinase at 102-103 higher inhibitor concentrations in spite of the significant homology between these protein tyrosine kinases.These results demonstrate the ability to synthesize selective tyrosine kinase inhibitors.The most potent EGF receptor kinase inhibitors also inhibit the EGF-dependent proliferation of A431/clone 15 cells with little or no effect on EGF independent cell growth.These results demonstrate the potential use of protein tyrosine kinase inhibitors as selective antiproliferative agents for proliferative diseases caused by the hyperactivity of protein tyrosine kinases.We have suggested the name "tyrphostins" for this class of antiproliferative compounds which act as protein tyrosine kinase blockers.

Heteroatom Rearrangements. Extension to Aliphatic Carboxylic Acids

2-Cyano-3-mercapto-3-(methylthio)acrylamide condenses with aliphatic carboxylic acids in the presence of polyphosphoric acid trimethylsilyl ester to give the corresponding 1,3-thiazin-4-ones (S,N double unrearranged products); under the same conditions, 3