Our laboratory has reported the development of bifunctional catalysts where a helical peptide backbone enables precise control over intercatalyst distances for the design of enzyme-like catalytic processes. In this study, we report the effect of varying intercatalyst distance by moving a second catalytic group from the i+4 to the i+3, i+5, and i+7 positions.  We verify the helicity of each peptide catalysis with CD spectroscopy and confirm inter-catalyst interactions via 2-D NMR studies.  The catalytic efficiency of each catalyst is also reported in model organic transformations.

Structural effects on catalysis with bifunctional, enzyme-like, helical peptide catalysts

251st National Meeting (2016)

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