Monosaccharide-Mediated Glycoxidation of Bovine Serum Albumin and Its Prevention by .

The substantial rise in metabolic illnesses that has occurred in both developed and developing countries over the last three decades has been linked to an increase in sugar-added foods and sweetened beverage intake. The significance of advanced glycation end products (AGEs) in the pathophysiology of metabolic diseases related to modern nutrition is an emerging issue. Spices and herbs can potentially be potent AGE production inhibitors due to their high polyphenol content. The inhibitory activity of an aqueous extract of seeds (NS) on glucose- and fructose-mediated glycation of bovine serum albumin (BSA) was investigated. The glycation of proteins and its prevention using NS were assessed using spectrophotometry, spectrofluorometrics, and electrophoretic techniques. Additionally, the NBT assay, DNPH assay, Ellman assay, and thioflavin T assay were used to observe the biochemical alterations caused by glycated BSA. Molecular docking was employed to dock the BSA active site residues with inhibitors. Our data showed that NS protects against glucose- and fructose-mediated glycation and aggregation in vitro by inhibiting the formation of fructosamine, protein carbonyl content, free sulfhydryl groups, and fluorescent AGEs. Furthermore, NS also inhibited the production of β-cross-amyloid aggregates in proteins. It was interesting to note that the inhibition was found to be significantly higher in the Glu-BSA system, although the glycation product formed in the Fru-BSA system was higher compared to the Glu-induced protein system. It can be concluded that, by inhibiting AGE production, oxidation, and aggregation of the protein, NS may be an effective antiglycation drug for the prevention of diabetes complications.