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Peroxiredoxins are a widely conserved family of enzymes that function in antioxidant defense and act in redox signaling pathways. Increased expression of human peroxiredoxin is associated with cancer, cardiovascular dysfunction, and neurodegeneration. Conoidin A inactivates peroxiredoxins by covalently binding to the catalytic cysteine on the enzyme.1,2 It has been shown to inhibit peroxiredoxin II (IC50 = 23 µM) in the parasite T. gondii and peroxiredoxin I in the hookworm A. ceylanicum.1,2,3 At 5 µM, conoidin A can also inhibit the glucose oxidase-
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1. Identification of conoidin A as a covalent inhibitor of peroxiredoxin II. Org. Biomol. Chem. 7, 3040-3048 (2009).
2. Peroxiredoxin-
3. Optimisation of conoidin A, a peroxiredoxin inhibitor. ChemMedChem 5(1), 41-45 (2010).