This review provides an overview of glycation, a non-enzymatic process where reducing sugars or their autoxidation products react with amino groups of proteins, DNA, or lipids, leading to the formation of advanced glycation end products (AGEs). The formation of AGEs can affect the biological function of biomacromolecules and contribute to the development of various diseases, including obesity, diabetes-related conditions, coronary artery disease, neurological disorders, and chronic renal failure. The review discusses the molecular mechanisms underlying glycation reactions, the bio-molecular targets prone to glycation, and the effects of AGEs on protein structure, function, and aggregation. It also explores the role of computational chemistry in understanding these effects and reviews the most prevalent diseases induced by glycation, along with current therapeutic interventions. The introduction highlights the historical context of glycation, from its discovery in 1912 to its recognition as a significant factor in diabetic-related diseases. The review emphasizes the differences between glycation and glycosylation, the molecular mechanisms of glycation, and the impact of glycation on protein structure and function. It also discusses the interplay between glycation and protein aggregation, and the potential role of glycation in neurodegenerative diseases. Finally, the review covers the use of computational chemistry to study the effects of glycation on protein structure and function, providing insights into the complex dynamics of this process.This review provides an overview of glycation, a non-enzymatic process where reducing sugars or their autoxidation products react with amino groups of proteins, DNA, or lipids, leading to the formation of advanced glycation end products (AGEs). The formation of AGEs can affect the biological function of biomacromolecules and contribute to the development of various diseases, including obesity, diabetes-related conditions, coronary artery disease, neurological disorders, and chronic renal failure. The review discusses the molecular mechanisms underlying glycation reactions, the bio-molecular targets prone to glycation, and the effects of AGEs on protein structure, function, and aggregation. It also explores the role of computational chemistry in understanding these effects and reviews the most prevalent diseases induced by glycation, along with current therapeutic interventions. The introduction highlights the historical context of glycation, from its discovery in 1912 to its recognition as a significant factor in diabetic-related diseases. The review emphasizes the differences between glycation and glycosylation, the molecular mechanisms of glycation, and the impact of glycation on protein structure and function. It also discusses the interplay between glycation and protein aggregation, and the potential role of glycation in neurodegenerative diseases. Finally, the review covers the use of computational chemistry to study the effects of glycation on protein structure and function, providing insights into the complex dynamics of this process.