In addition, these ROS are involved in several pathological processes such as atherosclerosis and cancer. Therefore, this enzyme is an important source of superoxide radicals and hydrogen peroxide, which contributes to oxidative stress and takes part in the aging process. Physiologically, XO catalyzes the oxidative hydroxylation of hypoxanthine and xanthine into uric acid (UA) with the concomitant production of reactive oxygen species (ROS). Xanthine oxidase (XO) is a molybdoflavoprotein widely disseminated throughout the human body, and is present in the liver, intestine, lungs, kidneys, heart, brain, and plasma. In silico molecular properties such as drug-likeness, pharmacokinetics, and toxicity of this promising barbiturate were also analyzed and herein discussed. The most powerful bis-thiobarbiturate within this set showed in vitro IC 50 of 1.79 ОјM, which was about ten-fold better than Allo inhibition, together with suitable low cytotoxicity. In general, all bis-thiobarbiturates present a good antioxidant performance and an excellent ability to inhibit XO at a concentration of 30 ВµM, eight of them are superior to those observed with the reference drug allopurinol (Allo), nevertheless they were not as effective as febuxostat. With this in mind, sixteen bis-thiobarbiturates were synthesized in moderate to excellent reactional yields, and their antioxidant, anti-proliferative, and XO inhibitory activity were evaluated. This great diversity of biological activities is directly linked to the enormous opportunities found for chemical change off the back of these findings.

However, in recent years a very large group of potential pharmaceutical and medicinal applications have been related to their structure. Barbiturates and their congeners thiobarbiturates represent a class of heterocyclic drugs capable of influencing neurotransmission. Therefore, this enzyme has been associated with pathological conditions caused by hyperuricemia, such as the disease commonly known as gout. Xanthine oxidase (XO) is the enzyme responsible for the conversion of endogenous purines into uric acid.

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