Study on human serum albumin modified by glucose with proteomic technique

Advanced glycation end products (AGEs) are a heterogeneous group of complex compounds which may play a role in the pathogenesis of chronic complications associated with diabetes complications, renal failure and aging. Human Serum Albumin (HSA) is the most abundant protein in blood serum. Glucose has the ability to modify HSA and other proteins through glycation. This study was carried out on glycated HSA which was analyzed by LC/MS with the aim of identifying specific peptides. Analysis of the LC/MS data showed that there were differences between peptides of glycated and normal HSA. Modification sites of glycated peptides were also studied. These typical peptides were considered as biomarkers for clinical diagnose of diabetes and aging.