Comparative Approach of Modification of Human Serum Albumin and the Dynamics of the Advanced Glycation End Products Formation

Glycation of protein produces advanced glycation end products (AGEs) that alter their biological activity. Many of the complications are linked with the non‐enzymatic glycation of proteins. Both reducing sugars and dicarbonyl compounds show strong affinity for human serum albumin (HSA), which is the most abundant protein in serum. Aim : The purpose of this study is a comparative analysis of the alteration of HSA and the dynamics of the formation of AGEs. Method : We systemically investigated the dynamics of the in vitro AGEs formation by various spectroscopic techniques. Major findings : The glycation pattern of HSA was found to vary with the glycating agent property, and the impact of oxidative stress and glycative stress on HSA comparatively leads to different changes in HSA properties. Conclusion : Our preliminary study provide important insights into the structural perturbations in protein by analyzing the biomarkers of both the stress using physicochemical techniques.