اثر مهاركنندگي آلانتوئين بر گلايكيشن هموگلوبين انساني

Non-enzymatic glycation is the process of binding reducing sugars to the amine moiety of proteins, which over time leads to the production of advanced glycation end products (AGEs) an‎d serious damage to the structure an‎d function of proteins such as hemoglobin. In this study, allantoin (due to its guanidine-like structure similar to metformin) with known antioxidant properties, reactive oxygen species (ROS) inhibition, an‎d free radical suppression was used to protect hemoglobin against AGE damage. The changes in the primary to tertiary structures of ribosylated hemoglobin in the presence of allantoin were eva‎luated an‎d compared with metformin. ThT an‎d ANS fluorescence spectroscopy, UV-Visible spectroscopy, an‎d Concord assay were used to follow protein conformational changes. TNBS, DTNB, an‎d DNPH-2,4 reagents were used to eva‎luate changes in lysine, cysteine, an‎d carbonyl groups. The results showed that compared to metformin, allantoin significantly protects the conformation an‎d structure of hemoglobin against the destructive effect of ribose, an‎d the formation of Hb-AGEs. Molecular docking studies showed a higher affinity of allantoin (based on a more negative binding energy an‎d more hydrogen bonds) for its binding site in hemoglobin. According to the presented findings, the superiority of allantoin over metformin in preserving the structure an‎d conformation of hemoglobin during ribosylation was determined

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