Folded proteins perform diverse functions in biological systems.  Most of these operations require the polypeptide chain to adopt a specific conformation.  Over the past two decades there has been growing interest in the prospect that protein functions might be recapitulated and perhaps even improved upon with unnatural oligomers that manifest discrete folding preferences.  Such systems are referred to generically as "foldamers".  Protein-inspired foldamers include molecules with backbones built from extended subunits such as beta-amino acids ("beta-peptides") or gamma-amino acids ("gamma-peptides").  Newer efforts have involved heterogeneous peptidic backbones, i.e., backbones in which different types of subunits are combined, such as "alpha/beta-peptides" and "alpha/beta/gamma-peptides".  Some of these systems, alpha/beta-peptides in particular, allow mimicry of information-rich surfaces displayed by natural polypeptides.  The resulting foldamers can inhibit specific protein-protein interactions, or they can augment signaling through polypeptide-activated receptors.  Recent results in this area will be described.

Mimicry of biorecognition motifs with peptidic foldamers

249th National Meeting (2015)

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