David Smith

Document Type

Honors Thesis


The Maillard reaction has garnered attention in a wide variety of industries in chemistry, including food science, textiles, and pharmaceuticals. Most recently, the Maillard reaction has become medically relevant, mediating the irreversible addition of sugars to proteins. This non-enzymatic post-translational modification, called glycation, leads to the formation of advanced glycation end products (AGEs). AGE formation steadily increases with age and is known to mediate the pathogenesis of numerous agerelated diseases including cardiovascular, renal, ocular, and neurodegenerative diseases, especially in diabetic or uremic patients. The mechanisms of pathogenesis for these diseases, as well as the full extent of the impact of AGE accumulation, is not fully understood. This study aims to identify proteins susceptible glycation in human plasma through phenylglyoxal treatment and LC-MS analysis. Thirty proteins were identified, about half of which were susceptible to glycation. Various avenues to increase protein and glycation identification are discussed.

Publication Date






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