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Updated: Apr 28, 2026

Metabolic Glycoengineering of Sialic Acid Using N-acyl-modified Mannosamines
Published on: November 25, 2017
Glycation at the Crossroads of Disease Pathogenesis: Mechanistic Insights and Therapeutic Frontiers
Sneha Krishnamoorthi1, Rupachandra Saravanakumar1, Vivek Kumar1
1Department of Biotechnology, School of Bioengineering, SRM Institute of Science and Technology, Kattankulathur, Chengalpattu 603 203, Tamil Nadu, India.
Abstract:
Protein glycation is a nonenzymatic modification that links sugar chemistry to molecular aging and chronic disease. Sequential reactions involving Schiff bases, Amadori products, and reactive α dicarbonyl intermediates generate advanced glycation end products (AGEs) that irreversibly alter protein structure and function. AGEs also act as ligands for the receptor for advanced glycation end products (RAGE), initiating oxidative stress, inflammation, and tissue remodeling. This review synthesizes the molecular pathways of AGE formation, their structural diversity, and the biological factors influencing glycation kinetics. Advances in analytical detection methods-including fluorescence spectroscopy, LC-MS/MS, and immunochemical approaches-are highlighted for their role in monitoring AGE accumulation. Particular attention is given to the contribution of glycation to diabetes, cardiovascular disease, neurodegeneration, and cancer, alongside emerging therapeutic strategies to limit AGE formation or block AGE-RAGE signaling. Glycation thus represents a central mechanism in human disease pathogenesis and an emerging therapeutic frontier.
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