ORGN 710 |
| We are investigating the design, synthesis and activity of artificial esterases and aldolases. We have developed a system based on a polymeric backbone, which possesses multiple catalytic and binding sites to confer a statistical advantage for catalysis. The artificial esterases consist of dipeptide binding groups and a histidine catalytic group coupled to a polyallylamine backbone. The rate of ester hydrolysis was demonstrated to be solvent, pH and substrate concentration dependent. The design of artificial aldolases has focused on the generation of chiral ß-ketosulfoxides as transition state analogues. Their binding affinity towards selected dipeptides has been investigated. This strategy for the assembly of artificial enzymes allows us to explore the contributing factors that are responsible for enzyme catalysis. Furthermore, this will enable us to develop mild catalytic processes for which there are no natural enzymes available. |
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Asymmetric Reactions, Molecular Recognition, Self Assembly, Bioorganic Chemistry, Process R&D
8:00 PM-10:00 PM, Wednesday, 16 March 2005 Convention Center -- Hall D, Poster
Division of Organic Chemistry |