Molecular self-assembly is a process ubiquitous in nature that refers to the spontaneous assembly of
molecules in order to generate supramolecular structures through noncovalent interactions. Such a natural mechanism
can be mimicked to modulate the fabrication of novel materials. The secret underlying the production of successful
self-assembled materials lies on the careful selection of its building blocks. Control over the final architecture
may be achieved by adjusting the size, shape and surface chemistry of these building blocks. Peptides are
promising candidates as monomers for self-assembly, in part, due to the variety of amino acids which comprise different
chemical functionalities. Such chemical diversity allows several interactions to take place, such as hydrogen bonding, hydrophobic
effects or electrostatic interactions. In addition to design versatility, an increasing understanding of protein and peptide folding mechanisms
allows the rational design of the monomer and its final assembly. Peptides have great potential for biomedical applications due to
their inherent biocompatibility and biodegradability. In fact, self-assembled peptide-based biomaterials have been developed for the production
of 3D scaffolds for tissue repair and regeneration and therapeutic drug delivery. Since peptides are bioactive molecules, its applications
may go far beyond the fabrication of inactive architectures. Inherently functional materials may also be produced. In this review,
we explore the different strategies adopted by scientists in the fabrication of peptide-based self-assembled biomaterials and provide a
comprehensive overview of the mechanisms governing it.
Keywords: Beta-sheet, biomaterials, coiled-coil, peptides, self-assembly, supramolecular chemistry, therapeutics.
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