Advanced glycation end products (AGEs) are formed when glucose glycates plasma proteins through a non-enzymatic process, leading to the development of diabetic complications such as retinopathy, nephropathy, neuropathy, and cardiomyopathy. This review discusses the glycation of plasma proteins like albumin, fibrinogen, globulins, and collagen, and their role in the pathogenesis of these complications. The formation of AGEs involves the Maillard reaction, which can be divided into early, intermediate, and late stages. AGEs interact with receptors for advanced glycation end products (RAGE), altering intracellular signaling, gene expression, and the release of pro-inflammatory molecules and free radicals. The accumulation of AGEs in tissues and their interaction with RAGE contribute to the progression of diabetic complications. Recent studies suggest that pharmacological interventions targeting AGEs or RAGE can potentially prevent or delay the onset of these complications.Advanced glycation end products (AGEs) are formed when glucose glycates plasma proteins through a non-enzymatic process, leading to the development of diabetic complications such as retinopathy, nephropathy, neuropathy, and cardiomyopathy. This review discusses the glycation of plasma proteins like albumin, fibrinogen, globulins, and collagen, and their role in the pathogenesis of these complications. The formation of AGEs involves the Maillard reaction, which can be divided into early, intermediate, and late stages. AGEs interact with receptors for advanced glycation end products (RAGE), altering intracellular signaling, gene expression, and the release of pro-inflammatory molecules and free radicals. The accumulation of AGEs in tissues and their interaction with RAGE contribute to the progression of diabetic complications. Recent studies suggest that pharmacological interventions targeting AGEs or RAGE can potentially prevent or delay the onset of these complications.