We report the use of short a-helical polypeptides as scaffolds for the construction of enzyme-like multifunctional catalysts. The helical amino acid backbone provides a structurally rigid, tunable template for incorporation of multiple catalysts in close proximity to one another. The peptide backbone can also be modified to tune the local environment around each catalyst, providing a new method for optimizing reaction efficiency in an enzyme-like manner. In this report we will describe our efforts to incorporate transition metals, Lewis acids, hydrogen bonding and organo-catalysts onto our helical template for the development of novel and efficient multifunctional catalysts. We also report that close proximity of the catalyst to the helical template can minimize the influence of solvent on the selectivity of organo-catalytic Diels-Alder reactions. This preliminary data suggests that the template structure can shield the incorporated catalysts, creating an enzyme-like environment for the development of new catalytic transformations.

Helical peptide scaffolds for the development of enzyme-like catalysts

248th National Meeting (2014)

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