50700-55-5

Basic information

• Product Name: 1-Methyl-2-nitro-1H-iMidazole-5-carboxylic acid
• Synonyms: 1-Methyl-2-nitro-1H-iMidazole-5-carboxylic acid;1H-IMidazole-5-carboxylic acid, 1-Methyl-2-nitro-;1-Methyl-2-nitro-1H-iMidazole-5-carboxylic acid-6;EOS-61726
• CAS NO: 50700-55-5
• Molecular Formula: C₅H₅N₃O₄
• Molecular Weight: 171.1109
• Mol File: 50700-55-5.mol
• Article Data: 6

Chemical Properties

• Boiling Point: 493.9±37.0 °C(Predicted)
• Appearance: /
• Density: 1.72±0.1 g/cm3(Predicted)
• Storage Temp.: Sealed in dry,Room Temperature
• PKA: 2.44±0.26(Predicted)
• CAS DataBase Reference: 1-Methyl-2-nitro-1H-iMidazole-5-carboxylic acid(CAS DataBase Reference)
• NIST Chemistry Reference: 1-Methyl-2-nitro-1H-iMidazole-5-carboxylic acid(50700-55-5)
• EPA Substance Registry System: 1-Methyl-2-nitro-1H-iMidazole-5-carboxylic acid(50700-55-5)

Safety Data

• Hazardous Substances Data: 50700-55-5(Hazardous Substances Data)

Usage

General Description

1-Methyl-2-nitro-1H-imidazole-5-carboxylic acid is a chemical compound with the molecular formula C7H6N4O4. It is an organic compound that contains a nitro group, imidazole ring, and carboxylic acid group. 1-Methyl-2-nitro-1H-iMidazole-5-carboxylic acid is commonly used as an intermediate in the synthesis of pharmaceuticals and agrochemicals. It is also used in the manufacturing of dyes, pigments, and other organic compounds. The chemical has potential applications in the medical and agricultural industries due to its unique structure and properties. Additionally, it is important to handle this compound with caution, as it may pose health and environmental risks if not properly managed.

Upstream product

• 39070-13-8 ethyl 1-N-methyl-2-nitro-1H-imidazole-5-carboxylate 
• 40361-77-1 2-amino-1-methyl-1H-imidazole-5-carboxylic acid methyl ester 
• 40361-79-3 1-methyl-2-nitro-1H-imidazole-5-carboxylic acid methyl ester 

Downstream Products

• 67855-45-2 (6R)-3-methyl-7t-(3-methyl-2-nitro-3H-imidazole-4-carbonylamino)-8-oxo-(6rH)-5-thia-1-aza-bicyclo[4.2.0]oct-2-ene-2-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 
• 39928-74-0 1-methyl-2-nitro-1H-imidazole-5-carbaldehyde 
• 246536-87-8 (1-methyl-2-nitro-1H-imidazol-5-yl)methyl (4-nitrophenyl) carbonate 

Relevant articles and documents

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.

Design, synthesis and evaluation of imidazolylmethyl carbamate prodrugs of alkylating agents

Two approaches to prodrugs of alkylating agents based on an imidazolylmethyl carbamate nucleus were explored. A 2-azido analogue (3) of the bis-carbamate carmethizole (1) displayed similar aerobic cytotoxicity to 1 in a panel of human and murine cell lines. Approaches to the 2-amino and 2- carbamoyl analogues are described. In the second approach an imidazolylmethanol was used as a 'trigger' linked via a carbamate to the alkylating agent N,N-bis(2-chlorethyl)amine (BCEA). Nitroimidazole and methylsulphinylimidazole carbamate prodrugs 6-8 were 5-20-fold less toxic than BCEA. Despite this deactivation in the prodrug form, little increase in cytotoxicity was observed under hypoxia. The data suggest that BCEA released on bioreduction is not sufficiently potent to contribute significant additional cytotoxicity. (C) 2000 Elsevier Science Ltd.