69976-81-4

Usage

Preparation

Preparation by diazotization of 6-amino-3-hydroxy-2- methylacetophenone, followed by hydrolysis of the obtained diazonium salt in the presence of hypophosphorous acid at 0° (42%).

Upstream product

• 24487-92-1 1-(3-methoxy-2-methylphenyl)ethanone 
• 55289-06-0 3-methoxy-2-methylbenzoic acid 
• 603-80-5 3-hydroxy 2-methylbenzoic acid 
• 917-54-4 methyllithium 

Downstream Products

• 1192215-69-2 2-bromo-1-(3-hydroxy-2-methylphenyl)ethanone 
• 1196732-39-4 N-[1-(2-methyl-3-hydroxyphenyl)ethyl]-ethane-1,2-diamine 

Relevant academic research and scientific papers

Activity-Based Proteome Profiling Probes Based on Woodward's Reagent K with Distinct Target Selectivity

Woodward's reagent K (WRK) is a reactive heterocyclic compound that has been employed in protein chemistry to covalently and unspecifically label proteins at nucleophilic amino acids, notably at histidine and cysteine. We have developed a panel of WRK-der

8-AZABICYCLO[3.2.1]OCTANE-8-CARBOXAMIDE DERIVATIVE

Disclosed is a compound represented by formula (1) or a pharmacologically acceptable salt thereof (In the formula, A represents a group that is represented by formula (A-1); R1a and R1b may be the same or different and each independently represents a C1-6 alkyl group which may be substituted by one to three halogen atoms; m and n each independently represents an integer of 0-5; X1 represents a hydroxyl group or an aminocarbonyl group; Z1 represents a single bond or the like; and R2 represents an optionally substituted C1-6 alkyl group, an optionally substituted C6-10 aryl group or the like.)

10A-AZALIDE COMPOUND HAVING 4-MEMBERED RING STRUCTURE

A 10a-azalide compound having a 4-membered ring structure crosslinked at the 10a- and 12-positions, which is represented by the formula (I), and is effective on even Haemophilus influenzae, or erythromycin resistant bacteria (e.g., resistant pneumococci and streptococci).

Structure-based optimization of potent and selective inhibitors of the tyrosine kinase erythropoietin producing human hepatocellular carcinoma receptor B4 (EphB4)

The tyrosine kinase EphB4 is an attractive target for drug design because of its recognized role in cancer-related angiogenesis. Recently, a series of commercially available xanthine derivatives were identified as micromolar inhibitors of EphB4 by high-throughput fragment-based docking into the ATP-binding site of the kinase domain. Here, we have exploited the binding mode obtained by automatic docking for the optimization of these EphB4 inhibitors by chemical synthesis. Addition of only two heavy atoms, methyl and hydroxyl groups, to compound 4 has yielded the single-digit nanomolar inhibitor 66, with a remarkable improvement of the ligand efficiency from 0.26 to 0.37 kcal/(mol per non-hydrogen atom). Compound 66 shows very high affinity for a few other tyrosine kinases with threonine as gatekeeper residue (Abl, Lck, and Src). On the other hand, it is selective against kinases with a larger gatekeeper. A 45 ns molecular dynamics (MD) simulation of the complex of EphB4 and compound 66 provides further validation of the binding mode obtained by fragment-based docking. 2009 American Chemical Society.