Protein-protein interactions play important roles in the pathogenesis of many diseases, but are notoriously difficult to perturb using small molecules. Therefore, peptoids (N-alkylglycine oligomers) have been developed to inhibit these interactions by binding to the relevant protein-protein interfaces. Unfortunately, the conformational preferences of typical peptoids are often suboptimal for their binding to polyproline-binding signaling proteins because most peptoid side chains engender cis-amides in the peptoid backbone, while known polyproline ligands typically form PPII helices defined by trans-amide conformations. This talk will describe our efforts to address this important challenge through the development of new PPII helix mimics containing tertiary thioamide, or �thiopeptoid�, residues, which are predicted to engage in strong intra- and intermolecular interactions that will promote trans-thioamides, PPII-type helix formation, and protein binding. Progress towards the synthesis of peptoid catalysts for the enantioselective trifluoromethylation of carbonyl groups will also be presented.

Synthesis of peptoid/thiopeptoid hybrids as polyproline type II helix mimics

247th National Meeting (2014)

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