Glykation

Glykation, also called glycation, is the non-enzymatic reaction of reducing sugars with free amino groups in proteins, lipids, or nucleic acids. The process begins with formation of a reversible Schiff base between a carbonyl group of a reducing sugar and a primary amine (commonly the amino group of lysine residues or the N-terminus). The Schiff base can undergo Amadori rearrangement to form a more stable ketoamine, often referred to as an early glycation product. Over time, these early products undergo complex rearrangements, oxidation, and dehydration to yield advanced glycation end products (AGEs).

Physiological relevance: Glycation occurs endogenously, at low rates, but rates increase with hyperglycemia, aging, and oxidative stress. Dietary intake of preformed AGEs also contributes.

Impact: AGEs can cross-link proteins, alter structure and function, and interact with cellular receptors such as RAGE, initiating inflammatory signaling, oxidative stress, and vascular damage. Clinically, glycated hemoglobin HbA1c is a common biomarker of long-term glucose control; higher AGE burden is associated with diabetes complications and may play a role in aging and neurodegeneration.

Prevention and study: Approaches to reduce AGE formation include better glycemic control and minimizing intake or cooking methods that produce dietary AGEs; research explores AGE inhibitors and breakers, though clinical adoption is limited.