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Interaction with other helices is possible through the side chains of the amino acids involved, as they protrude outwards from the helix. The α-helical structure results from hydrogen bonding between backbone amides that form right-handed α-helices with a periodicity of 3.6 residues per turn. However, with the advent of material design, only recently have key molecules been discovered in order to incorporate these helical structures into biomaterials. We believe that this review highlights the importance of self-assembled peptide nanostructures for nanomedicine applications and can facilitate further knowledge and understanding of these nanosystems towards clinical translation of such therapeutic materials.įor decades it has been known that physical and biological properties can promote the formation of helical structures. Finally, we also cover a broad range of self-assembled peptides and peptide derivatives. We aim to provide insight into how SAPs can be engineered into smart drug-delivery platforms that exhibit enhanced biological functions, such as intracellular and targeting uptake, controlled release, and reversible enzymatic hydrogel formation. The focus of this review is on factors that govern self-assembled peptide (SAP) targeting activity, and controlled-release properties. Therefore, there is a lack of comprehensive reviews on the use of self-assembled peptides as “smart” drug-delivery platforms that are capable of specific tissue or cellular targeting, and release of therapeutic components in response to environmental cues. Though there has been several reviews on peptides and their self-assembling properties, most are focused on tissue engineering rather than drug-delivery applications. Self-assembly is important in cell-penetrating peptide (CPP) mechanisms, which play a major role in introducing drugs inside cell membranes and translocating genes inside a nucleus. Although several self-assembly platforms have been introduced for biomedical applications, self-assembling peptides remain the most attractive soft biomaterial option for several reasons: Self-assembling nanostructures fabricated from natural biomolecular building blocks such as amino acids are highly preferable to their synthetic self-assembled monolayer (SAMs) alternatives due to their biocompatibility and ease of “bottom-up” fabrication. Self-assembly occurs spontaneously in nature during protein folding, DNA double-helix formation, and the formation of cell membranes. Self-association to form hierarchical structures at both the nano and/or microscales occurs in order to achieve these energy minima. Hydrogen bonding, hydrophobic interactions, electrostatic interactions, and van der Waals forces combine to maintain molecules at a stable low-energy state. These processes occur under thermodynamic and kinetic conditions that are a consequence of specific and local molecular interactions. Molecular self-assembly is the spontaneous formation of ordered structures.