Synthesis and Bioactivity Study of Novel Hybrid Antioxidant
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Purpose: Antioxidant enzymes are the first line defense for preventing oxidative stress (OS) by scavenging free radicals, and different enzymes scavenge different reactive oxygen species (ROS). We focused on two major antioxidants: superoxide dismutase (SOD), which removes superoxide; and glutathione peroxidase (GPx), which removes hydrogen peroxide radicals. The purpose was to synthesize a hybrid compound with multiple antioxidant activities and to test the total ROS scavenging ability using a chemical assay. The goal is to use this class of compound as a method of preventing and treating ophthalmologic diseases related to oxidative damage. Methods: Synthesis of a hybrid antioxidant MN-1-26 was carried out using an amide coupling reaction between 4-amino Tempol (a SOD mimetic) and NHBoc methionine followed by purification using liquid chromatography. Structure confirmation was done using proton NMR. The ROS scavenging chemical assay was conducted following a literature protocol where pyrogallol was used as the ROS generator. Changes in UV absorbance were measured at different time points to compare MN-1-26 (250µm) with SA-2 (a known SOD mimetic) and Baicalein (a polyphenolic antioxidant) as positive controls. Result: Compound MN-1-26 has the correct chemical structure, determined by proton NMR, with the highest superoxide scavenging ratio (28%) at 90 minutes compared to SOD mimetic SA-2 (22%), and Baicalein (24%). Conclusion: The hybrid antioxidant demonstrated superior ROS scavenging activity over individual antioxidants. Further cellular studies of MN-1-26 are under progress, with the goal of reducing OS and cell death in vitro.