The development of multifunctional catalysts can enable enzyme-like reactivity by bringing multiple reactive intermediates into close proximity and enabling proximity-accelerated reactivity. Our laboratory recently demonstrated that an alpha-helical peptide can be used to scaffold multiple catalysts and enable this type of proximity-induced reactivity. In this report, we describe our efforts to optimize the length and stability of the peptide scaffold, and the distance between the two helix-bound catalysts in order to maximize catalyst performance. We also investigate the impact of proximal side chain residues on the enantioselectivity of catalysts bound to the helical peptide template. These effects are investigated in the context of enantioselective Diels-Alder and Indole Alkylation reactions.<br/>

Optimizing the enzyme-like reactivity of a bifunctional helical peptide catalyst

255th National Meeting (2018)

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