![]() These interactions underlie the formation of two major secondary structural motifs designated as α-helix and β-sheet. The self-assembly is mainly driven by different noncovalent interactions such as hydrogen bonding, electrostatic attraction, and van der Waals forces. The self- assembly of peptides and their various analogues has been employed to prepare diverse interesting nanostructures, including fibers, tubes, ribbons, vesicle, films, and three-dimensional (3D) networks, which have been utilized for diverse functional purposes, such as drug delivery, tissue engineering, sensing, optoelectronics, catalysis, and biotechnology. In addition, the wide range of available amino acids allows to modify the physical and chemical properties by varying the primary structures, adjusting them to specific applications. In this context, peptides are attractive building blocks because of their simple synthesis, rich chemical diversity and inherent biocompatibility. However, the exploitation of protein self-assembly to fabricate desired materials is extremely challenging due their complex nature and the difficulties in controlling the self-assembly process. Inspired by this ubiquitous use of proteins by nature, a number of self-assembled artificial materials have been developed. In natural biological systems, self-assembled proteins nanostructures play diverse key roles, such as the self-assembled molecular structure of the actin cytoskeleton, which provides physical rigidity to the cell, self-assembled microtubules that allow the transport of cargo within the cells, and self-assembled collagen fibers, the most abundant component in the Extracellular Matrix (ECM), which play an essential role in cell adhesion and growth. We focus on the association between self-assembled mesoscale structures and their material function and demonstrate the way by which this class of building blocks bears the potential for diverse applications, such as the future fabrication of smart devices.īiomolecular self-assembly into controllable nanostructures has recently emerged as an exciting direction of research to fabricate materials with novel functional properties. Here, we outline the func-tional roles of self-assembled nanostructures formed by short helical peptides and their potential as artificial materials. ![]() Similar to β-sheet structures, short helical peptides have been recently discovered to possess a diverse set of func-tionalities with the potential to fabricate artificial self-assembling materials. ![]() In con-trast, collagen, the most abundant protein in mammals, is based on helical arrangement. Likewise, many natu-ral proteinaceous materials, such as silk and amyloid fibrils, are based on β-sheet structures. The formation of β-sheet organizations by short peptides is well explored, leading to the development of a wide range of functional assemblies. ![]() The self-assembly of short peptide building blocks into well-ordered nanostructures is a key direction in bionanotechnology. ![]()
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