1033752-64-5

Usage

Chemical class

Piperazine class of organic compounds

Structure

Piperazine ring with a 6-methoxypyridin-2-yl substituent at one end and a 4-methyl substituent at the other

Potential applications

Drug discovery and pharmaceutical research

Use

Building block in the synthesis of biologically active molecules

Context dependency

Properties and potential uses may vary depending on the specific context and application

Further research

May be needed to fully understand its potential uses and effects
Please note that this list is based on the provided material and may not be exhaustive. Further research and analysis may reveal additional properties and applications for 1-(6-methoxypyridin-2-yl)-4-methylpiperazine.

Upstream product

• 109-01-3 1-methyl-piperazine 
• 17228-64-7 6-chloro-2-methoxypyridine 
• 40473-07-2 6-bromo-2-methoxypyridine 

Downstream Products

• 1268274-19-6 3-((2-methoxy-6-(4-methylpiperazin-1-yl)pyridin-3-yl)thio)aniline 
• 1268274-20-9 N-(3-((2-methoxy-6-(4-methylpiperazin-1-yl)pyridin-3-yl)thio)-phenyl)propionamide 
• 1268274-21-0 N-(3-((2-methoxy-6-(4-methylpiperazin-1-yl)pyridin-3-yl)thio)-phenyl)cyclopropanecarboxamide 
• 1268274-22-1 2-amino-N-(3-((2-methoxy-6-(4-methylpiperazin-1-yl)pyridin-3-yl)thio)phenyl)acetamide 
• 1311934-33-4 C₂₄H₃₃N₅O₄S 
• 1567951-04-5 N-(3-((2-methoxy-6-(4-methylpiperazin-1-yl)pyridin-3-yl)thio)-phenyl)benzamide 
• 612498-68-7 6-(4-methylpiperazin-1-yl)pyridin-2-ol 
• 1567951-13-6 1-(6-((4-methoxybenzyl)oxy)pyridin-2-yl)-4-methylpiperazine 
• 1567951-16-9 1-(5-iodo-6-((4-methoxybenzyl)oxy)pyridin-2-yl)-4-methylpiperazine 
• 1567951-19-2 3-((2-((4-methoxybenzyl)oxy)-6-(4-methylpiperazin-1-yl)pyridin-3-yl)thio)aniline 
• 1567951-22-7 2-amino-N-(3-((2-hydroxy-6-(4-methylpiperazin-1-yl)pyridin-3-yl)thio)phenyl)acetamide 

Relevant academic research and scientific papers

Heat shock protein 70 inhibitors. 2. 2,5′-thiodipyrimidines, 5-(phenylthio)pyrimidines, 2-(pyridin-3-ylthio)pyrimidines, and 3-(phenylthio)pyridines as reversible binders to an allosteric site on heat shock protein 70

The discovery and development of heat shock protein 70 (Hsp70) inhibitors is currently a hot topic in cancer. In the preceding paper in this issue (10.1021/jm401551n), we have described structure-activity relationship studies in the first Hsp70 inhibitor class rationally designed to bind to a novel allosteric pocket located in the N-terminal domain of the protein. These ligands contained an acrylamide to take advantage of an active cysteine embedded in the allosteric pocket and acted as covalent protein modifiers upon binding. Here, we perform chemical modifications around the irreversible inhibitor scaffold to demonstrate that covalent modification is not a requirement for activity within this class of compounds. The study identifies derivative 27c, which mimics the biological effects of the irreversible inhibitors at comparable concentrations. Collectively, the back-to-back manuscripts describe the first pharmacophores that favorably and selectively interact with a never explored pocket in Hsp70 and provide a novel blueprint for a cancer-oriented development of Hsp70-directed ligands.

HEAT SHOCK PROTEIN BINDING COMPOUNDS, COMPOSITIONS, AND METHODS FOR MAKING AND USING SAME

The present subject matter relates to a compound represented by the general formula (I) or (I') or a pharmacologically acceptable salt thereof; pharmaceutical compositions containing at least one of these compounds; methods of making at least one of these compounds; methods of using at least one of these compounds for treating and/or preventing various cancers and/or proliferation disorders; methods of using at least one of these compounds for monitoring the effectiveness of an anticancer therapy against various cancers. In one embodiment, the subject matter relates to compounds that bind with a level of specificity to heat shock protein 70 (Hsp70). In another embodiment, the subject matter relates to compounds that bind with a level of specificity to inhibit both heat shock protein 70 (Hsp70) and heat shock cognate protein 70 (Hsc70).

Pd-catalyzed aryl amination mediated by well defined, N-heterocyclic carbene (NHC)-Pd precatalysts, PEPPSI

Pd-N-heterocyclic carbene (NHC)-catalyzed Buchwald-Hartwig animation protocols mediated by Pd-PEPPSI precatalysts is described. These protocols provide access to a range of hindered and functionalized drug-like aryl amines in high yield with both electron-deficient and electron-rich aryl- and heteroaryl chlorides and bromides. Variations in solvent polarity, base and temperature are tolerated, enhancing the scope and utility of this protocol. A mechanistic rationalization for base strength (pKb) requirements is also provided.