Aromatic garlands, as new foldamers, to mimic protein secondary structure

Proteins modulate the majority of all biological functions and are composed of highly organized secondary structural elements such as helices, turns, and sheets. Many of these functions are affected by a small number of key structural element, protein-protein interactions. Their mimicry by peptide and non-peptide scaffolds has become a major focus of contemporary research. This paper examines oligomeric system as new foldamers, which either reproduce the local topography of the helix, or project appropriately functionality in a similar manner to residues of an alpha-helix.

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