Glycation or a Maillard reaction is a post translational modification event which is the result of covalent bonding of a free amino group of proteins with a reducing sugar such as glucose and fructose which results in the formation of an early glycation product that undergoes rearrangement, dehydration and cyclization to form a more stable Amadori product (ketoamine). Both Schiff base and Amadori glycation products generate free radicals resulting in decline of antioxidant defence mechanisms which can damage cellular organelles and enzymes. Under high glucose load (hyperglycaemic condition), the Amadori products undergo a non-enzymatic glycation reaction leading to the formation of a complex series of compounds known as the Advanced Glycation End products (AGEs) via intermediate compounds, such as 3-Deoxyglucosone (3DG), Glyoxal (GO) and Methylglyoxal MG. Despite the fact that sugars are the main precursors of AGEs, these intermediary metabolites are also believed to participate in glycation reactions. Among these are 3-Deoxyglucosone (3-DG), known to be an important highly reactive dicarbonyl intermediate of the Maillard reaction; and Carboxymethyllysine (CML) and pentosidine as promoters of formation of AGEs. These intermediate compounds can also diffuse out of the cell and react with extracellular proteins. Excessive AGE accumulation results in significant cellular dysfunction by altering protein structure. Thus, 3DG, GO and MG are glycation intermediates and precursors of AGEs; and relevant targets for inhibitory compounds aimed to reduce the undesirable consequences of protein glycation both in vitro and in vivo. In addition to proteins, glycation affects a variety of other biomolecules containing free amino groups such as DNA and lipoproteins, thereby perturbing the structure and function of these biomolecules. The schematic representations of DNA glycation pathway along with protein and lipid macromolecule.