In diabetes mellitus (DM), non-enzymatic glycation of proteins, lipids, and
fatty acids is accelerated due to persistent hyperglycemia and plays an important role in
diabetes and its associated secondary complications. Glycation has the potential to alter
the biological, structural, and functional properties of macromolecules. Glycated
products (early and late) are both involved in provoking the immune-regulatory cells
and generating autoantibodies in diabetic patients. More precisely, human serum
albumin is the most abundant protein in circulation involved in glycation. Glycated
albumin may accumulate in the body tissues of diabetic patients and participate in its
secondary complications. This chapter compiles the studies focused on changes in the
secondary and tertiary structure of proteins upon glucosylation. Various in-vitro and
in-vivo approaches involved in investigating such changes are systematically reviewed.
Besides, the potential role of glycated albumin in the pathogenesis of diabetes mellitus,
as well as its applicability as a diagnostic marker in the progression of the disease, is
also highlighted.
Keywords: Hyperglycemia, Non-enzymatic glycation, Glycated Albumin, Protein glycation, Diabetes.
