Abstract by Michael Nielsen
Chemistry and Biochemistry
Development of an Enzyme-inspired Bis-thiourea Catalyst
The development of enzyme-inspired catalysts is a focus of the Michaelis Laboratory. I am currently working on a series of peptide-based thiourea catalysts that enhance the rate and enantioselectivity of anion abstraction chemistry. The Jacobson group at Harvard recently demonstrated that by creating a scaffold to properly orient two thiourea catalysts they were able to obtain a 96% yield and 92% ee. We have designed a 14 amino acid, helical peptide that we will use as a scaffold to create a thiourea catalyst and a bis-thiourea catalyst. We hypothesize that the secondary structure of the peptide will provide a scaffold that will orient the two thiourea catalysts to optimize reactivity. We will test the reactivity of a butyl thiourea catalyst, a monofunctional peptide-based catalyst, and a bis-thiourea peptide-based catalyst. High reactivity is expected from the bis-thiourea peptide-based catalyst because the structure of the peptide will orient the two thiourea catalysts in a highly reactive manner.