161053-91-4

Upstream product

• 119-36-8 methyl salicylate 
• 161053-66-3 ethyl 2-<(2-methoxyethoxy)methoxy>-β-oxobenzenepropanoate 
• 1026424-77-0 Imidazol-1-yl-[2-(2-methoxy-ethoxymethoxy)-phenyl]-methanone 
• 161053-75-4 3-(3-Bromo-propoxy)-benzoic acid ethyl ester 
• 81254-82-2 methyl 2-[(2-methoxyethoxy)methoxy]benzoate 
• 81254-83-3 2-<(2-methoxyethoxy)methoxy>benzoic acid 
• 7781-98-8 ethyl-3-hydroxybenzoate 
• 1027016-08-5 3-{4-Ethoxycarbonyl-5-[2-(2-methoxy-ethoxymethoxy)-phenyl]-5-oxo-pentyloxy}-benzoic acid ethyl ester 

Relevant academic research and scientific papers

Coumarin derivatives as protease inhibitors and antiviral agents

The present invention relates to novel coumarin derivatives and related compounds which potently inhibit the HIV aspartyl protease blocking HIV infectivity. The coumarin derivatives are useful in the development of therapies for the treatment of viral infections and diseases, including AIDS. The present invention is also directed to methods of synthesis of multifunctionalized coumarins and of related structures.

A novel nonpeptide HIV-1 protease inhibitor: Elucidation of the binding mode and its application in the design of related analogs

HIV-1 protease has been identified as a significant target enzyme in AIDS research. While numerous peptide-derived inhibitors have been described, the identification of a nonpeptide inhibitor remains an important goal. Using an HIV-1 protease mass screening technique, 4-hydroxy-3-(3-phenoxypropyl)-2H-1- benzopyran-2-one (1) was identified as a nonpeptide competitive inhibitor of the enzyme. Employing a Monte Carlo-based docking procedure, the coumarin was docked in the active site of the enzyme, revealing a binding mode that was later confirmed by the X-ray crystal analysis. Several analogs were prepared to test the binding interactions and improve the overall binding affinity. The most active compound in the study was 4,7-dihydroxy-3-[4-(2- methoxyphenyl)butyl]-2H-1-benzopyran-2-one (31).