Xanthine Oxidase (XO) is an enzyme responsible for the conversion of hypoxanthine to xanthine to uric acid and for the generation of Reactive Oxygen Species (ROS) found within the blood and lungs. These ROS are the cause of reperfusion injuries that follow the reintroduction of oxygen after an ischemic event, such as a myocardial infarction or stroke. Two classes of compounds were investigated for their ability to inhibit xanthine oxidase and scavenge ROS. The first class of compounds is known as chalcones, with the second being analogues of caffeic acid phenethyl ester (CAPE). The ability of these compounds to inhibit xanthine oxidase was determined by measuring the rate of uric acid production using spectroscopic methods. Computational docking was used to identify crucial inhibitor/receptor interactions and to visualize inhibitor binding at the molecular level. Additional assays with the stable free radical 2,2-diphenyl-1-picrylhydrazyl were carried out to measure the radical scavenging capacity of the chalcone and CAPE derivatives. Many of the tested compounds possessed at least one of the two desirable properties, with some being able to fulfill both objectives. In addition to the two in vitro methods, in vivo cell viability assays were performed to assess a compound’s ability to reduce oxidative stress in neuro-2a cells exposed to Beta-amyloid peptide.

Chalcones and analogs of caffeic acid phenethyl ester with xanthine oxidase inhibiting and radical scavenging properties: Tools capable of suppressing oxidative stress in cells

249th National Meeting (2015)

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