618881-38-2

Basic information

• Product Name: methyl [3-amino-4-(hept-1-ynyl)-6-methyl]benzoate
• Synonyms: methyl [3-amino-4-(hept-1-ynyl)-6-methyl]benzoate
• CAS NO: 618881-38-2
• Molecular Weight: 259.348
• Mol File: 618881-38-2.mol

Chemical Properties

• CAS DataBase Reference: methyl [3-amino-4-(hept-1-ynyl)-6-methyl]benzoate(CAS DataBase Reference)
• NIST Chemistry Reference: methyl [3-amino-4-(hept-1-ynyl)-6-methyl]benzoate(618881-38-2)
• EPA Substance Registry System: methyl [3-amino-4-(hept-1-ynyl)-6-methyl]benzoate(618881-38-2)

Safety Data

• Hazardous Substances Data: 618881-38-2(Hazardous Substances Data)

Upstream product

• 77324-87-9 methyl 2-methyl-5-nitrobenzoate 
• 18595-12-5 methyl 5-amino-2-methylbenzoate 
• 628-71-7 1-Heptyne 
• 686342-80-3 methyl (3-amino-4-iodo-6-methyl)benzoate 

Downstream Products

• 782499-32-5 methyl [3-hydroxymethyl-2-(1-pentyl)-1-(2-phenylethyl)-5-methyl]indole-6-carboxylate 
• 618881-41-7 methyl [3-formyl-2-pentyl-1-(2-phenylethyl)-5-methyl]indole-6-carboxylate 

Relevant articles and documents

Small molecule inhibition of a PDZ-domain interaction

Novel compounds that have been found effective in inhibiting PDZ domain interactions, and particularly interactions of PDZ domains in MAGIs with the oncogenic (tumor suppressor) protein PTEN and interactions between the PDZ domain in the Dishevelled (Dvl) protein and other proteins such as the Frizzled (Fz) protein, have the general formula The invention also includes combinatorial libraries, arrays and methods for screening and studying proteins using such compounds. Compounds of the invention have produced apoptosis in certain cell lines that overexpress the Dishevelled protein (Dvl); inhibiting Wnt signaling.

A selective irreversible inhibitor targeting a PDZ protein interaction domain

Irreversible inhibitors of proteases have proven themselves useful tools for determining which proteases are active under given conditions in tissues or cells and for studying the functional role that a protease plays in physiological processes. The application of such techniques to the study of the activity and function of protein-protein interactions has been hindered by the lack of guiding principles for the mechanistic design of irreversible inhibitors targeting the "active site" of a protein interaction. We report herein the first example of a mechanism-based irreversible inhibitor of a protein interaction that has been specifically targeted to one member of the PDZ family of protein interaction domains: the second PDZ domain of the membrane-associated guanylate kinase MAGI3. This inhibitor was designed using rationally directed computational evaluation to take advantage of a conserved histidine in the PDZ domain by introducing an ionizable group that will be held in close proximity to that nucleophile during binding. The novel compound exhibits all of the characteristics of an irreversible inhibitor of the interaction of the tumor suppressor PTEN with MAGI3 in in vitro models. In cells, the inhibitor can be shown to release PTEN from sequestration by MAGI3 and consequently upregulate the PKB signaling pathway. Copyright