Although many cellular processes depend on enzymatic reactions, protein–protein interactions (PPIs) mediate many regulatory pathways—the explosion of interest in their study mirrors a key role in diseased states. 1 Small molecules that selectively target PPIs are therefore urgently required. 2, 3 What is not clear is how to achieve inhibition using a small molecule, given that it must cover B800–1100 Aof a protein surface and complement the discontinuous projection of hydrophobic and charged domains on a relatively shapeless surface. 4 In the proteomimetic5 approach a scaffold is used to project binding functionality in an identical spatial orientation to mimic that presented by a given secondary structure (commonly an α-helix) involved in the interaction. 6 In addition to Hamilton’s terphenyl, 5, 7 a number of proteomimetic scaffolds have been described. 8–15 Similarly, foldamers, 16 if suitably designed, function as inhibitors of PPIs. 17–19 Aromatic oligoamides are particularly attractive as foldamers because they exhibit predictable folding patterns controlled largely by the preferred conformation of the Aryl–NHCO–Aryl bond and adjacent ortho interactions; 20, 21 however, such foldamers have rarely been shown to act as α-helix mimicking antagonists of