glycationa

Glycation, also known as non-enzymatic glycosylation, is a biochemical process where reducing sugars or their derivatives react with amino groups in proteins, lipids, or nucleic acids. This reaction forms stable adducts called **advanced glycation end-products (AGEs)**, which accumulate over time in living organisms. The process is a normal part of metabolism but becomes significant in conditions of prolonged hyperglycemia, such as diabetes mellitus.

The initial step of glycation involves the condensation of a sugar molecule, typically glucose or fructose, with a free amino group on proteins or lipids, forming a labile Schiff base. This intermediate rearranges into a more stable Amadori product. Over time, further rearrangements and oxidations lead to the formation of AGEs, which can alter protein structure and function. Glycation affects collagen, hemoglobin, and other key biomolecules, contributing to long-term complications in diabetes, such as nephropathy, retinopathy, and cardiovascular disease.

AGEs can also form through the Maillard reaction, a process that occurs during cooking and aging of foods, contributing to the browning and flavor development in baked goods and roasted meats. While dietary AGEs may have health implications, including inflammation and oxidative stress, their impact is less direct than endogenous glycation.

Research into glycation has highlighted its role in aging and age-related diseases. Strategies to mitigate glycation include controlling blood sugar levels, consuming antioxidants, and limiting exposure to dietary AGEs. Enzymes like glyoxalase I and II play a protective role by breaking down early glycation intermediates, reducing AGE formation. Understanding glycation mechanisms continues to inform therapeutic approaches for diabetes and related conditions.