Abstract
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.
Graphical Abstract
Call for Papers in Thematic Issues
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