Foldamers are oligomers able to fold in stable conformational structure thanks to specific attractive or repulsive interactions between sites remote in sequences, like solvophobic effects, hydrogen bonding, local conformational restrictions, internal constrain or other stabilizing interactions. The comprehension of these properties and the possibility to design and synthesise specific sequences are of great importance in medicinal chemistry, especially to target protein-protein interaction domains, an approach of increasing interest in science.