• amphiphiles
• gycopeptoid
• peptoid
• self-assembly

Peptoids are peptidomimetic oligomers composed of N-substituted glycine units. For their intrinsically modular nature and easy synthesis, they represent an extremely promising choice for a systematic study of glyco-conjugates. The advantage with respect to peptides is that peptoids do not have extensive hydrogen bonding interactions on the backbone as a result of the N-substituents; diminishing, therefore, the energetic penalty for desolvating tertiary amides. Moreover, it is now possible to control the cis/trans isomerism of the backbone tertiary amide of peptoids, which otherwise might have shown conformational lability. Conjugated with different sugars they might give access to a new library of amphiphilic molecules, amphiphilic peptoids (APOs), with self-assembly properties in aqueous media. It is possible to modify the length of hydrophobic chains, the nature of polar groups, the nature of capping groups and sequential position of the residues to “tune” the physical properties of new self-assembled materials, like micelles, vesicles, membranes etc. Many applications can be envisioned for the use of APOs, like drug delivery, artificial membranes and stabilization and crystallization of membrane proteins.