Alok Raghav and Jamal Ahmad
Aligarh Muslim University, India
Posters & Accepted Abstracts: J Diabetes Metab
Non-enzymatic glycation involves rearrangement and covalent attachment of reducing sugars to reactive residues in proteins. HSA incubated for 40 days, conferred the formation of advanced glycation end products (AGEs) that play role in progression of immunological complications. We present an approach using high pressure liquid chromatography, CHNS analysis, scanning electron microscopy, X-ray diffraction, fluorescence to identify AGEs that were further used as probe to detect antibodies in serum of diabetes mellitus patients with type 2 (T2DM), type 1(T1DM), gestational (GDM) and type 2 with chronic kidney disease (T2DM+CKD) with direct binding and inhibition ELISA. Affinity purified immunoglobulin G (IgG) further probe to determine specificity with direct binding and inhibition ELISA. Biophysical analysis of native and glycated HSA showed severe damage to its structure and function. High titre of antibodies and percent inhibition was found in following order T2DM+CKD>T2DM>GDM>T1DM compared to healthy. Similarly affinity purified IgG showed high specificity in following order T2DM+CKD>T2DM>GDM>T1DM compared to healthy. Glycation alters the structure and function of HSA that imparts the formation of neoepitopes, recognized as foreign bodies by immune cells and formed autoantibodies that prove to be novel biomarker for detection of immunological progressive complications associated with diabetes mellitus.
Email: alokalig@gmail.com
