79566-30-6

Upstream product

• 29682-12-0 1-[4-(benzyloxy)-2-hydroxyphenyl]ethanone 
• 109-94-4 formic acid ethyl ester 
• 261529-75-3 7-(benzyloxy)-2-hydroxy-3,4-dihydro-2H-1-benzopyran-4-one 
• 59887-89-7 7-hydroxy-4H-chromen-4-one 
• 100-39-0 benzyl bromide 
• 100-44-7 benzyl chloride 
• 89-84-9 2',4'-dihydroxy-4-acetophenone 

Downstream Products

• 76240-27-2 7-hydroxy-2,3-dihydro-4H-chromen-4-one 
• 1373355-24-8 C₂₄H₂₀O₃ 
• 118975-25-0 7-acetoxy-2,3-dihydro-3-(4-methoxybenzylidene)-1-benzopyran-4-one 
• 83162-84-9 Bonducellin 
• 31042-20-3 7-(benzyloxy)chroman-4-one 

Relevant academic research and scientific papers

Selected C7-substituted chromone derivatives as monoamine oxidase inhibitors

A series of C7-substituted chromone (1-benzopyran-4-one) derivatives were synthesized and evaluated as inhibitors of recombinant human monoamine oxidase (MAO) A and B. The chromones are structurally related to a series of C7-functionalized coumarin (1-benzopyran-2-one) derivatives which has been reported to act as potent MAO inhibitors. The results of the current study document that the chromones are highly potent reversible inhibitors of MAO-B with IC50 values ranging from 0.008 to 0.370 μM. While the chromone derivatives also exhibit affinities for MAO-A, with IC50 values ranging from 0.495 to 8.03 μM, they are selective for the MAO-B isoform. Structure-activity relationships (SAR) show that 7-benzyloxy substitution of chromone is suitable for MAO-B inhibition with tolerance for a variety of substituents and substitution patterns on the benzyloxy ring. It may be concluded that 7-benzyloxychromones are appropriate lead compounds for the design of reversible and selective MAO-B inhibitors. With the aid of modeling studies, potential binding orientations and interactions of selected chromone derivatives in the MAO-A and -B active sites are examined.

Simplified catechin-gallate inhibitors of HIV-1 reverse transcriptase

Systematic simplification of the molecular structures of epicatechin gallate and epigallocatechin gallate to determine the minimum structural characteristics necessary for HIV-1 reverse transcriptase inhibition in vitro resulted in several compounds that strongly inhibited the native as well as the A17 double mutant (K103N Y181C) enzyme, which is normally insensitive to most known nonnucleoside inhibitors.

Structure of bonducellin, a naturally occuring 3-benzylidene-2,3-dihydro-1-benzopyran-4-one

2,3-Dihydro-7-hydroxy-3-(4-methoxybenzylidene)-1-benzopyran-4-one (1) and 2,3-dihydro-3-(4-hydroxybenzylidene)-7-methoxy-1-benzopyran-4-one (2) have been synthesized in order to confirm the structure of bonducellin, occuring in Caesalpinia bonducella and