39066-07-4

Usage

Uses

Used in Organic Synthesis:
1-(3,4-Dimethoxyphenyl)-valeronitrile is used as an intermediate in organic synthesis for the creation of various chemical compounds. Its unique structure allows for further functionalization and modification, making it a versatile building block in the development of new molecules.
Used in Medicinal Chemistry Research:
In the field of medicinal chemistry, 1-(3,4-Dimethoxyphenyl)-valeronitrile is used as a key intermediate in the synthesis of novel drugs and pharmacologically active compounds. Its potential pharmaceutical applications are being explored, with a focus on leveraging its structural features to design and develop new therapeutic agents.
Used in Drug Discovery:
1-(3,4-Dimethoxyphenyl)-valeronitrile is also utilized in drug discovery processes, where its biological activity and potential therapeutic properties are investigated. The presence of the dimethoxyphenyl group may enhance its interactions with biological targets, making it a promising candidate for the development of new medications.
Overall, 1-(3,4-Dimethoxyphenyl)-valeronitrile is a chemical compound with diverse applications in the fields of chemistry and drug discovery, making it an important tool for researchers and scientists working on the development of new pharmaceuticals and chemical compounds.

Upstream product

• 71-23-8 propan-1-ol 
• 93-17-4 3,4-dimethoxyphenylacetonitrile 
• 74-96-4 ethyl bromide 

Downstream Products

• 1616284-90-2 5-chloro-2-(3,4-dimethoxy-phenyl)-2-propyl-pentanenitrile 

Relevant academic research and scientific papers

Structure and Biocatalytic Scope of Coclaurine N-Methyltransferase

Benzylisoquinoline alkaloids (BIAs) are a structurally diverse family of plant secondary metabolites, which have been exploited to develop analgesics, antibiotics, antitumor agents, and other therapeutic agents. Biosynthesis of BIAs proceeds via a common pathway from tyrosine to (S)-reticulene at which point the pathway diverges. Coclaurine N-methyltransferase (CNMT) is a key enzyme in the pathway to (S)-reticulene, installing the N-methyl substituent that is essential for the bioactivity of many BIAs. In this paper, we describe the first crystal structure of CNMT which, along with mutagenesis studies, defines the enzymes active site architecture. The specificity of CNMT was also explored with a range of natural and synthetic substrates as well as co-factor analogues. Knowledge from this study could be used to generate improved CNMT variants required to produce BIAs or synthetic derivatives.

Synthesis of new verapamil analogues and their evaluation in combination with rifampicin against Mycobacterium tuberculosis and molecular docking studies in the binding site of efflux protein Rv1258c

New verapamil analogues were synthesized and their inhibitory activities against Mycobacterium tuberculosis H37Rv determined in vitro alone and in combination with rifampicin (RIF). Some analogues showed comparable activity to verapamil and exhibited better synergies with RIF. Molecular docking studies of the binding sites of Rv1258c, a M. tuberculosis efflux protein previously implicated in intrinsic resistance to RIF, suggested a potential rationale for the superior synergistic interactions observed with some analogues.