A series of 2-thiazolylhydrazone derivatives have been investigated for the ability to inhibit the activity of the A and B isoforms of monoamine oxidase (MAO) selectively. All of the compounds showed high activity against both the MAO-A and the MAO-B isoforms with pKi values ranging between 5.92 and 8.14 for the MAO-A and between 4.69 and 9.09 for the MAO-B isoforms. Both the MAO-A and the MAO-B isoforms, deposited in the Protein Data Bank as model 2BXR and 1GOS, respectively, were considered in a computational study performed with docking techniques on the most active and MAO-B-selective inhibitor, 18.
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Article Synopsis
- Monoamine oxidases (MAOs) are mitochondrial enzymes that create hydrogen peroxide as a byproduct and have been linked to oxidative stress in heart and metabolic issues.
- This study examined the role of MAOs in oxidative stress within valvular tissues from 30 patients with severe primary mitral regurgitation, focusing on their interaction with angiotensin 2 (ANG2).
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