Self-assembly of Collagen Mimetic Peptides

Collagen mimetic peptides (CMPs) present promising synthetic alternatives to animal-derived collagen, boasting advantages like reduced risk of viral infection, low immunogenicity, and convenient quality control. However, mimicking collagen's intricate self-assembly process in short CMPs averaging only 10 nm presents significant challenges. This chapter delves into strategies for devising the self-assembly of short CMPs into homotrimers and heterotrimers to replicate collagen's structural characteristics. It thoroughly examines strategies for homotrimer peptide self-assembly, including diverse approaches such as amphiphilic interactions, π–π interactions, metal ion coordination, electrostatic interactions, triblock peptides, and covalent cross-linking, facilitating the creation of well-defined supramolecular architectures at the nano- and micro-scale, encompassing structures like fibers, microflorettes, meshes, microtubes, hollow spheres, nanodisks, and nanosheets. Additionally, innovative strategies involving covalent cross-linking, electrostatic interactions, and Ln3+-ligand interactions are explored to promote the self-assembly of heterotrimeric peptides into supramolecular structures. The chapter concludes by highlighting applications of self-assembled collagen mimetic peptides in cargo delivery, cell culture, and hemostatic applications, emphasizing their potential in various biomedical fields.