40361-77-1

Usage

Uses

Used in Pharmaceutical Synthesis:
Methyl 2-amino-3-methyl-imidazole-4-carboxylate is utilized as an intermediate in the production of pharmaceuticals. Its unique structure and functional groups contribute to the development of new drugs, enhancing their efficacy and therapeutic potential.
Used in Agricultural Chemicals:
methyl 2-amino-3-methyl-imidazole-4-carboxylate also serves as an intermediate in the synthesis of agricultural chemicals, where it plays a crucial role in the development of novel agrochemicals to improve crop protection and yield.
Used in Coordination Chemistry:
Methyl 2-amino-3-methyl-imidazole-4-carboxylate has been studied for its potential as a ligand in coordination chemistry. Its ability to form stable complexes with metal ions makes it a promising candidate for applications in catalysis, materials science, and other areas.
Used in Laboratory Research:
In the realm of scientific research, methyl 2-amino-3-methyl-imidazole-4-carboxylate is employed in laboratory settings for the exploration of new chemical processes and the synthesis of diverse organic compounds. Its reactivity and structural features facilitate the discovery of innovative chemical reactions and pathways.
Used in Chemical Process Development:
Methyl 2-amino-3-methyl-imidazole-4-carboxylate is integral to the development of new chemical processes, where its properties and reactivity are harnessed to create more efficient and sustainable methods for the synthesis of various organic compounds.

InChI:InChI=1/C6H9N3O2/c1-9-4(5(10)11-2)3-8-6(9)7/h3H,1-2H3,(H2,7,8)

Upstream product

• 420-04-2 CYANAMID 
• 40361-84-0 2-(formyl-methyl-amino)-3-oxo-propionic acid methyl ester 

Downstream Products

• 50700-55-5 1-methyl-2-nitro-1H-imidazole-5-carboxylic acid 
• 39070-14-9 1-methyl-2-nitro-5-hydroxymethylimidazole 
• 304015-66-5 (1-methyl-2-nitro-1H-imidazol-5-yl)methyl (4-(hydroxymethyl)phenyl)carbamate 
• 304016-33-9 (1-methyl-2-nitro-1H-imidazol-5-yl)methyl (4-((((4-nitrophenoxy)carbonyl)oxy)methyl)phenyl)carbamate 
• 40361-79-3 1-methyl-2-nitro-1H-imidazole-5-carboxylic acid methyl ester 
• 918633-87-1 evofosfamide 

Relevant academic research and scientific papers

Rational Design for Nitroreductase (NTR)-Responsive Proteolysis Targeting Chimeras (PROTACs) Selectively Targeting Tumor Tissues

The catalytic properties of proteolysis targeting chimeras (PROTACs) may lead to uncontrolled off-tissue target degradation that causes potential toxicity, limiting their clinical applications. The precise control of this technology in a tissue-selective manner can minimize the potential toxicity. Hypoxia is a hallmark of most solid tumors, accompanied by elevated levels of nitroreductase (NTR). Based on this character, we presented a type of NTR-responsive PROTACs to selectively degrade proteins of interest (POI) in tumor tissues. Compound 17-1 was the first NTR-responsive PROTAC synthesized by incorporating the caging group on the Von Hippel-Lindau (VHL) E3 ubiquitin ligase ligand. It could be activated by NTR to release the active PROTAC 17 to efficiently degrade the EGFR protein and subsequently exert antitumor efficacy. Thus, a general strategy for the precise control of PROTAC to induce POI degradation in tumor tissues by NTR was established, which provided a generalizable platform for the development of NTR-controlled PROTACs to achieve selective degradation.

Targeting a Targeted Drug: An Approach Toward Hypoxia-Activatable Tyrosine Kinase Inhibitor Prodrugs

Tyrosine kinase inhibitors (TKIs), which have revolutionized cancer therapy over the past 15 years, are limited in their clinical application due to serious side effects. Therefore, we converted two approved TKIs (sunitinib and erlotinib) into 2-nitroimidazole-based hypoxia-activatable prodrugs. Kinetics studies showed very different stabilities over 24 h; however, fast reductive activation via E. coli nitroreductase could be confirmed for both panels. The anticancer activity and signaling inhibition of the compounds against various human cancer cell lines were evaluated in cell culture. These data, together with molecular docking simulations, revealed distinct differences in the impact of structural modifications on drug binding to the enzymes: whereas the catalytic pocket of the epidermal growth factor receptor (EGFR) accepted all new erlotinib derivatives, the vascular endothelial growth factor receptor (VEGFR)-inhibitory potential in the case of the sunitinib prodrugs was dramatically diminished by derivatization. In line, hypoxia dependency of ERK signaling inhibition was observed with the sunitinib prodrugs, while oxygen levels had no impact on the activity of the erlotinib derivatives. Overall, proof of principle could be shown for this concept, and the results obtained are an important basis for the future development of tyrosine kinase inhibitor prodrugs.