Amyotrophic Lateral Sclerosis (ALS) is a disease which affects about 1 out of every 300,000 people in the United States. This neurodegenerative disease removes motor function from the patient at an alarmingly fast rate, leaving a life expectancy of only 2-5 years. A true, universal cause of ALS is still largely unknown given the attention that the disease has had in recent years. One potential cause of ALS is a glycation reaction which inhibits protein function within the body and promotes inflammation. A glycation reaction is a one in which an amino acid or protein condenses with the carbonyl of a free carbohydrate to eventually form what is known as an advanced glycation end product (AGE).  While AGEs have long been known as causal factors with respect to inflammatory response and chronic disease (e.g., arthritis, heart disease, neurodegenerative disorders), little is understood about chemistry behind AGE formation.  The goal of this research was to study how simple amino acids react with common sugars to model the formation of AGEs in the body. Various combinations were tested by reacting the D-form of simple carbohydrates (Fructose, Galactose, Glucose or Mannose) and an aryl amine or amino acid (Aspartic Acid, Tryptophan, Aniline, Phenylalanine, Benzylamine).   These glycation reactions were run under mild conditions (40 degrees C, 3-4 hours, with acetic acid).  Products were isolated as air-stable white solids in reasonable yield (65-80%) and characterized by IR, NMR and Mass Spectrometry.  NMR analysis did confirm the expected presence of both the alpha- and beta-anomer product.<br/>

Glycation reactions and their application towards ALS identification and treatment

255th National Meeting (2018)

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