Recent Advances in Peptoids: Synthesis, Self‐Assembly, and Applications

Peptoids, or N ‐substituted glycine oligomers, have emerged as a highly versatile class of peptidomimetic materials owing to their structural diversity, chemical stability, and tunable functionality. Advances in synthetic methodologies have enabled precise sequence control and conformational tuning, allowing for the rational design of peptoids with predictable folding and assembly characteristics. Recent research has focused on elucidating the self‐assembly mechanisms of peptoids, which are governed by the interplay of hydrophobic interactions, π–π stacking, hydrogen bonding, and backbone chirality. These cooperative noncovalent interactions give rise to a wide range of hierarchical nanostructures, including nanosheets, nanofibers, and helical ribbons, depending on side‐chain functionality and solvent environment. The resulting architectures exhibit remarkable structural robustness and functionality, opening avenues for diverse applications in nanotechnology, catalysis, drug delivery, and biosensing. Furthermore, their exceptional stability under physiological environments makes peptoid‐based assemblies attractive candidates for biomedical and environmental uses. This review highlights recent advances in peptoid synthesis, self‐assembly, and functional applications, emphasizing their growing potential as programable peptidomimetic systems for next‐generation supramolecular and biomimetic materials.