CHED 352 |
| Asymmetric synthesis of amino acids has important applications in chemistry, biology, and medicine. Most amino acids are biosynthesized via the transaminase enzyme family, utilizing the cofactor pyridoxal/pyridoxamine phosphate. Recently, the Breslow group has reported the use of reduced-peptide-based polyamines as novel enantioselective transaminase mimics. Polymeric enzyme models are promising candidates for the catalysis of stereoselective reactions. These chiral polyamines can be synthesized through the reduction of polypeptides by BH3•THF. Only catalytic quantities of the peptide-based polyamines and of the modified pyridoxamine are required, and the reactions proceed under aqueous conditions. By emulating the strategies utilized by biological enzymes, including the hydrophobic effect, enzyme/substrate specificity, and increased effective molarity, a catalytic system with stereoselectivity as well as good rate enhancement and turnover will be developed. This biomimetic approach could serve as an environmentally friendly alternative in the asymmetric synthesis of α-amino acids. |
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Undergraduate Research Poster Session: Organic Chemistry
11:00 AM-1:00 PM, Monday, 27 March 2006 Georgia World Congress Center -- Ex. Hall B4, Poster
Division of Chemical Education |