Advanced Glycation Endproducts, (AGEs): Formation, Complication and Pharmacological Evaluation to Its Inhibition

Abstract

Glycation commonly known as non-enzymatic glycosylation is the result of sugar molecules binding with a protein or lipid molecule without controlling the action of an enzyme. During the process of glycation, early stage glycation compounds are formed first, which subsequently rearrange into final advanced glycation end products (AGEs) structures through a series of very complex chemical reactions and formed methylglyoxal-lysine dimer, glyoxallysine dimer and the deoxyglucosone-lysine dimer . AGEs are involved in many age related diseases such as type–II (diabetic mellitus), cardiovascular disease (the endothelial cell, collagen, fibrinogen are damaged), Alzheimer diseases (amyloid protein are side product of the reaction progressing to AGEs), Cancer (acryl-amide and other side product are related), peripheral neuropathy (the myelin is attached), and other sensory losses such as deafness (due to demyelination), and blindness (mostly due to micro-vascular damage in the retina), this span of diseases is the result of very root level at which glycation interfere with molecular and cellular functioning throughout the body. Pharmacologically influence the process of non-enzymatic glycation and AGE product formation Inhibit the formation of AGEs are purported to have therapeutic potentials in patients with hyperglycemia and age-related diseases. The redox process is believed to play an important role in AGEs formation The best cross-link inhibitors currently available are carnosine, aminoguanidine, metformin and acarbose, whereas others are now becoming available. No cross-link breakers are commercially obtainable as yet, but these will be marketed within 2-3 years. Soon after, combinations of inhibitors and breakers are due to follow.