Design, synthesis and biological evaluation of novel benzocoumarin derivatives as potent inhibitors of MAO-B activity.

The continued research of novel reversible inhibitors targeting monoamine oxidase (MAO) B remains crucial for effectively symptomatic treatment of Parkinson's disease. In this study we synthesized and evaluated a new series of 3-aryl benzo[g] and benzo[h] coumarin derivatives as MAO-B inhibitors. Compound A6 has been found to display the most potent inhibitory activity and selectivity against the MAO-B isoform (IC = 13 nM and SI = >7693.

DNA and hemoglobin binding activities: Investigation of coumarin-thiosemicarbazone hybrids.

Coumarin and coumarin-thiosemicarbazone hybrids were synthesized and characterized by various techniques such as FT-IR, H NMR, C NMR, MALDI-TOF-MS spectroscopy, and single crystal X-Ray diffractometer (XRD). The photochemical and photophysical properties of the compounds, such as solvatochromism, solubility, and chemical reactivity, were analyzed using UV-vis spectroscopy in different solvents. Due to the potential biological activities of the synthesized compounds, their binding affinity and mechanisms with calf thymus DNA (ct-DNA) and bovine hemoglobin (BHb) were determined using several useful spectrophotometric and theoretical approaches such as UV-vis absorption and fluorescence spectroscopy, molecular docking, and density functional theory (DFT).

Arylcoumarin and novel biscoumarin derivatives as potent inhibitors of human glutathione S-transferase.

A series of arylcoumarin derivatives and two novel biscoumarin derivatives were investigated for their human recombinant glutathione S-transferase P1-1 (GSTP1-1) enzyme inhibitory activities for the first time. 4-(3,4-Dihydroxyphenyl)-6,7-dihydroxycoumarin (compound ) was observed to be the most active coumarin derivative (IC: 0.14 µM).