33229-29-7

Upstream product

• 613-92-3 N-hydroxyl-benzamidine 
• 762-42-5 dimethyl acetylenedicarboxylate 
• 613-92-3 N-hydroxybenzenecarboximidamide 
• 100-47-0 benzonitrile 
• 613-92-3 N-hydroxybenzamidine 
• 613-92-3 (E)-N'-hydroxybenzimidamide 

Downstream Products

• 62222-36-0 methyl 5-hydroxy-6-oxo-2-phenyl-1,6-dihydropyrimidine-4-carboxylate 
• 62222-38-2 5,6-dihydroxy-2-phenyl-pyrimidine-4-carboxylic acid 
• 62222-36-0 methyl 5,6-dihydroxy-2-phenylpyrimidine-4-carboxylate 

Relevant academic research and scientific papers

Pharmacophore requirements for HIV-1 reverse transcriptase inhibitors that selectively “Freeze” the pre-translocated complex during the polymerization catalytic cycle

Reverse transcriptase (RT) is responsible for replicating the HIV-1 genome and is a validated therapeutic target for the treatment of HIV infections. During each cycle of the RT-catalyzed DNA polymerization process, inorganic pyrophosphate is released as the by-product of nucleotide incorporation. Small molecules were identified that act as bioisosteres of pyrophosphate and can selectively freeze the catalytic cycle of HIV-1 RT at the pre-translocated stage of the DNA- or RNA-template-primer-enzyme complex.

Design and discovery of 5-hydroxy-6-oxo-1,6-dihydropyrimidine-4-carboxamide inhibitors of HIV-1 integrase

Raltegravir (RAL) is a first clinically approved integrase (IN) inhibitor for the treatment of HIV but rapid mutation of the virus has led to chemo-resistant strains. Therefore, there is a medical need to develop new IN inhibitors to overcome drug resista

Rapid catalyst identification for the synthesis of the pyrimidinone core of HIV integrase inhibitors

A microscale chemistry improvement engine: A pre-dosed microscale high-throughput experimentation additives platform enables rapid, serendipitous reaction improvement. This platform allowed one chemist to set up 475 experiments and analyze the results using MISER chromatography in a single day, thus resulting in two high-quality catalytic systems for the construction of the title compound 1. Support for a single-electron transfer mechanism was obtained. Copyright

Dihydroxypyrimidine-4-carboxamides as novel potent and selective HIV integrase inhibitors

Human immunodeficiency virus type-1 (HIV-1) integrase, one of the three constitutive viral enzymes required for replication, is a rational target for chemotherapeutic intervention in the treatment of AIDS that has also recently been confirmed in the clinical setting. We report here on the design and synthesis of N-benzyl-5,6-dihydroxypyrimidine-4-carboxamides as a class of agents which exhibits potent inhibition of the HIV-integrase-catalyzed strand transfer process. In the current study, structural modifications on these molecules were made in order to examine effects on HIV-integrase inhibitory potencies. One of the most interesting compounds for this series is 2-[1-(dimethylamino)-1-methylethyl]-N-(4-fluorobenzyl)-5,6-dihydroxypyrimidine- 4-carboxamide 38, with a CIC95 of 78 nM in the cell-based assay in the presence of serum proteins. The compound has favorable pharmacokinetic properties in preclinical species (rats, dogs, and monkeys) and shows no liabilities in several counterscreening assays, highlighting its potential as a clinically useful antiviral agent.

Efficient synthesis of functionalized pyrimidones via microwave-accelerated rearrangement reaction

An efficient synthesis of functionalized pyrimidones via microwave-accelerated rearrangement reaction of amidoxime DMAD adducts is described. In most cases, the pyrimidone formation was furnished in reasonable yield after 2 min of microwave irradiation.