6630-30-4

Usage

Uses

Used in Pharmaceutical Industry:
6-Chloro-5-Nitropyrimidine-2,4-Diol is used as a key intermediate in the synthesis of pharmaceutical drugs for the treatment of various diseases. Its unique chemical structure allows for the development of new therapeutic agents with potential applications in cancer treatment, bacterial and viral infections, and other medical conditions. 6-Chloro-5-Nitropyrimidine-2,4-Diol's reactivity and functional groups enable the creation of diverse drug candidates with improved efficacy and selectivity.
Used in Agrochemical Industry:
In the agrochemical sector, 6-Chloro-5-Nitropyrimidine-2,4-Diol serves as a crucial building block for the synthesis of herbicides and insecticides. Its incorporation into these compounds enhances their biological activity, leading to more effective control of pests and weeds in agricultural settings. 6-Chloro-5-Nitropyrimidine-2,4-Diol contributes to the development of safer and more environmentally friendly agrochemicals by improving their target specificity and reducing non-specific impacts on the ecosystem.
Safety Considerations:
Due to its potential harmful effects on human health and the environment, it is essential to handle 6-Chloro-5-Nitropyrimidine-2,4-Diol with care. Proper safety measures, including the use of personal protective equipment, should be implemented during its synthesis, storage, and application to minimize exposure risks. Additionally, waste disposal and containment strategies should be in place to prevent environmental contamination.

InChI:InChI=1/C4H2ClN3O4/c5-2-1(8(11)12)3(9)7-4(10)6-2/h(H2,6,7,9,10)

Upstream product

• 4270-27-3 6-chlorouracil 

Downstream Products

• 13992-39-7 6-Cyclohexylamino-5-nitrouracil 
• 81964-31-0 6-(4-Chloranilino)-5-nitrouracil 
• 81964-32-1 6-(3-Fluoranilino)-5-nitrouracil 
• 81964-30-9 6-Anilino-5-nitrouracil 
• 81964-34-3 6-(4-Fluoranilino)-5-nitrouracil 
• 1173698-78-6 6-(2-hydroxybenzylamino)-5-nitropyrimidine-2,4(1H,3H)-dione 
• 343346-87-2 6-(benzylamino)-5-nitropyrimidine-2,4(1H,3H)-dione 
• 41964-42-5 5-Nitro-4-methylamino-uracil 

Relevant academic research and scientific papers

Synthesis and quantitative structure-activity relationship (QSAR) analysis of some novel oxadiazolo[3,4-d]pyrimidine nucleosides derivatives as antiviral agents

We have synthesized a series of 4H,6H-[1,2,5]oxadiazolo[3,4-d]pyrimidine-5,7-dione 1-oxide nucleoside and their anti-vesicular stomatitis virus (VSV) activities in Wish cell were also investigated in vitro. It was found that most compounds showed obvious anti-VSV activities and compound 9 with ribofuranoside improved the anti-VSV activity by approximately 10 times and 18 times compared to didanosine (DDI) and acyclovir, respectively. A quantitative structure-activity relationship (QSAR) study of these compounds as well as previous reported oxadiazolo[3,4-d]pyrimidine nucleoside derivatives indicated that compounds with high activity should have small values of log P(o/w), vsurf-G and a large log S value. These findings and results provide a base for further investigations.

Agonistic or antagonistic mucosal-associated invariant T (MAIT) cell activity is determined by the 6-alkylamino substituent on uracil MR1 ligands

Mucosal-associated invariant T (MAIT) are a subset of innate-like T cells that are activated by uracil ligands presented by MR1. For the first time, we demonstrate that changes to the 6-aminoalkyl chain on uracil agonist 5-OP-RU can determine agonistic or antagonistic MAIT cell activity. Insomuch, a simplified agonist with a functional profile similar to 5-OP-RU, and a new structural class of antagonist that exhibits similar activity to known MAIT cell antagonist Ac-6-FP, were identified. This journal is

The effect of MR1 ligand glyco-analogues on mucosal-associated invariant T (MAIT) cell activation

Mucosal-associated invariant T (MAIT) cells are a subset of recently identified innate-like T lymphocytes that appear to play an important role in many pathologies ranging from viral and bacterial infection, to autoimmune disorders and cancer. MAIT cells are activated via the presentation of ligands by MR1 on antigen presenting cells to the MAIT T cell receptor (TCR), however few studies have explored the effects of systematic changes to the ligand structure on MR1 binding and MAIT cell activation. Herein, we report on the first study into the effects of changes to the sugar motif in the known MAIT cell agonists 7-hydroxy-6-methyl-8-d-ribityllumazine (RL-6-Me-7-OH) and 5-(2-oxopropylideneamino)-6-d-ribitylaminouracil (5-OP-RU). Tetramer staining of MAIT cells revealed that the absence of the 2′-hydroxy group on the sugar backbone of lumazines improved MR1-MAIT TCR binding, which could be rationalised using computational docking studies. Although none of the lumazines activated MAIT cells, all 5-OP-RU analogues showed significant MAIT cell activation, with several analogues exhibiting comparable activity to 5-OP-RU. Docking studies with the 5-OP-RU analogues revealed different interactions between the sugar backbone and MR1 and the MAIT TCR compared to those observed for the lumazines and confirmed the importance of the 2′-hydroxy group for ligand binding and activity. Taken together, this information will assist in the development of future potent agonists and antagonists of MAIT cells.

Specific enzyme inhibitors in vitamin biosynthesis. Part 3. The synthesis and inhibitory properties of some substrates and transition state analogues of riboflavin synthase

Syntheses of potential inhibitors of riboflavin synthase are described. The tolerance of the enzyme to bulky substituents was investigated by the synthesis of substrate analogues which included lumazines and pyrido[2,3-d]-pyrimidines prepared by condensation of α-diketones and β-keto-aldehydes respectively with appropriate amino-substituted uracils. Potential transition-state analogues, including 7-oxolumazines, 7-oxopyrido[2,3-d] pyrimidines, and 6,7-dioxolumazines were also prepared by similar condensations using α-keto-acid derivatives, dimethyl acetylenedicarboxylate, and oxalate derivatives. Two possible dual affinity inhibitors were also prepared. The potential inhibitors were tested using riboflavin synthase from yeast or from E. coli, and their effectiveness is discussed in relation to the bulk and electronic character of the substituents.