371947-93-2

Usage

Uses

Used in Pharmaceutical Drug Development:
3-(4-Oxo-3,4-dihydroquinazolin-2-yl)phenyl acetate is utilized as a key component in the development of pharmaceutical drugs due to its potential biological activity and pharmacological properties. Its unique chemical structure allows it to interact with various biological targets, making it a valuable candidate for the treatment of various diseases and conditions.
Used in Medicinal Chemistry Research:
As a synthetic compound with potential biological activity, 3-(4-Oxo-3,4-dihydroquinazolin-2-yl)phenyl acetate serves as a valuable research tool in medicinal chemistry. It can be used to study the interactions between chemical compounds and biological targets, contributing to the understanding of disease mechanisms and the discovery of novel therapeutic agents.
Used in Chemical and Biological Studies:
3-(4-Oxo-3,4-dihydroquinazolin-2-yl)phenyl acetate is employed in chemical and biological studies to explore its potential applications and properties. Its quinazoline ring structure and acetate functional group provide a foundation for investigating its reactivity, stability, and interactions with other molecules, further expanding its utility in scientific research.

Upstream product

• 56071-04-6 2-(3-methoxyphenyl)quinazolin-4(3H)-one 
• 100-83-4 meta-hydroxybenzaldehyde 
• 28144-70-9 anthranilic acid amide 
• 134-20-3 2-carbomethoxyaniline 
• 1711-05-3 m-anisoyl chloride 
• 67836-50-4 2-[(3-methoxybenzoyl)amino]benzoic acid methyl ester 
• 330657-87-9 N-(2-carbamoylphenyl)-3-methoxybenzamide 
• 911417-23-7 2-(3-hydroxylphenyl)quinazolin-4(3H)-one 
• 108-24-7 acetic anhydride 

Downstream Products

• 1427578-95-7 2-(3-hydroxyphenyl)-3-(prop-2-yn-1-yl)quinazolin-4(3H)-one 
• 1427579-14-3 3-(4-azidobutyl)-2-(3-hydroxyphenyl)quinazolin-4(3H)-one 
• 1438417-42-5 3-(3-azidopropyl)-2-(3-hydroxyphenyl)quinazolin-4(3H)-one 
• 1427579-26-7 C₃₇H₃₁N₇O₅ 
• 1427579-33-6 2-(3-hydroxyphenyl)-3-((1-(4-(2-(4-hydroxyphenyl)-4-oxoquinazolin-3(4H)-yl)butyl)-1H-1,2,3-triazol-4-yl)methyl)quinazolin-4(3H)-one 
• 1427579-36-9 2-(4-hydroxyphenyl)-3-((1-(4-(2-(3-hydroxyphenyl)-4-oxoquinazolin-3(4H)-yl)butyl)-1H-1,2,3-triazol-4-yl)methyl)quinazolin-4(3H)-one 
• 1427579-42-7 C₃₆H₃₁N₇O₅ 
• 1427579-43-8 C₃₅H₂₉N₇O₅ 
• 1427579-80-3 C₃₇H₃₁N₅O₉ 
• 1427578-87-7 C₁₉H₁₄N₂O₃ 
• 911417-24-8 3-(4-chloroquinazolin-2-yl)phenyl acetate 

Relevant academic research and scientific papers

Studies on fragment-based design of allosteric inhibitors of human factor XIa

Human factor XIa (hFXIa) has emerged as an attractive target for development of new anticoagulants that promise higher level of safety. Different strategies have been adopted so far for the design of anti-hFXIa molecules including competitive and non-competitive inhibition. Of these, allosteric dysfunction of hFXIa's active site is especially promising because of the possibility of controlled reduction in activity that may offer a route to safer anticoagulants. In this work, we assess fragment-based design approach to realize a group of novel allosteric hFXIa inhibitors. Starting with our earlier discovery that sulfated quinazolinone (QAO) bind in the heparin-binding site of hFXIa, we developed a group of two dozen dimeric sulfated QAOs with intervening linkers that displayed a progressive variation in inhibition potency. In direct opposition to the traditional wisdom, increasing linker flexibility led to higher potency, which could be explained by computational studies. Sulfated QAO 19S was identified as the most potent and selective inhibitor of hFXIa. Enzyme inhibition studies revealed that 19S utilizes a non-competitive mechanism of action, which was supported by fluorescence studies showing a classic sigmoidal binding profile. Studies with selected mutants of hFXIa indicated that sulfated QAOs bind in heparin-binding site of the catalytic domain of hFXIa. Overall, the approach of fragment-based design offers considerable promise for designing heparin-binding site-directed allosteric inhibitors of hFXIa.

ALLOSTERIC MODULATORS OF FACTOR XIa AS ANTICOAGULANT AGENTS

Compounds which allosterically modulate and/or inhibit factor XIa activity are provided, as are methods of their use. These compounds include i) sulfated gallolyl glucosides, ii) sulfated quinazolinones, and iii) sulfated inositol analogs. The compounds used as anticoagulant agents.

Discovery of allosteric modulators of factor XIa by targeting hydrophobic domains adjacent to its heparin-binding site

To discover promising sulfated allosteric modulators (SAMs) of glycosaminoglycan-binding proteins (GBPs), such as human factor XIa (FXIa), we screened a library of 26 synthetic, sulfated quinazolin-4(3H)-ones (QAOs) resulting in the identification of six molecules that reduced the V max of substrate hydrolysis without influencing the KM. Mutagenesis of residues of the heparin-binding site (HBS) of FXIa introduced a nearly 5-fold loss in inhibition potency supporting recognition of an allosteric site. Fluorescence studies showed a sigmoidal binding profile indicating highly cooperative binding. Competition with a positively charged, heparin-binding polymer did not fully nullify inhibition suggesting importance of hydrophobic forces to binding. This discovery suggests the operation of a dual-element recognition process, which relies on an initial Coulombic attraction of anionic SAMs to the cationic HBS of FXIa that forms a locked complex through tight interaction with an adjacent hydrophobic patch. The dual-element strategy may be widely applicable for discovering SAMs of other GBPs.

RHO KINASE INHIBITORS

The present invention relates to inhibitors of ROCK1 and ROCK2, which may be selective for ROCK2, and methods of modulating the pharmacokinetic and/or pharmacodynamic properties of such compounds. Also provided are methods of inhibiting ROCK1 and/or ROCK2. Also provided are treatments combining inhibitors of ROCK1 and/or ROCK2 with statins.

RHO KINASE INHIBITORS

The present invention relates to inhibitors of ROCKl and R0CK2, which may be selective for R0CK2, and methods of modulating the pharmacokinetic and/or pharmacodynamic properties of such compounds. Also provided are methods of inhibiting ROCKl and/or R0CK2. Also provided are treatments combining inhibitors of ROCKl and/or R0CK2 with statins.

Synthesis and biological evaluation of 4-morpholino-2-phenylquinazolines and related derivatives as novel PI3 kinase p110α inhibitors

A series of 4-morpholino-2-phenylquinazolines and related derivatives were prepared and evaluated as inhibitors of PI3 kinase p110α. In this series, the thieno[3,2-d]pyrimidine derivative 15e showed the strongest inhibitory activity against p110α, with an

PHARMACOKINETICALLY IMPROVED COMPOUNDS

The present invention relates to inhibitors of ROCKl and R0CK2 and methods of modulating the pharmacokinetic and/or pharmacodynamic properties of such compounds. Also provided are methods of inhibiting ROCKl and or R0CK2 that are useful for the treatment of disease.