Self-assembly of surfactant-like peptides and their applications

Numerous peptides derived from naturally occurring proteins or de novo designed have been found to self-assemble into various nanostructures. These well-defined nanostructures have shown great potential for a variety of biomedical and biotechnological applications. In particular, surfactant-like peptides (SLPs) have distinctive advantages in their length, aggregating ability, and water solubility. In this article, we report recent advances in the mechanistic understanding of the self-assembly principles of SLPs and in their applications, most of which have been made in our laboratory. Hydrogen bonding between peptide backbones, hydrophobic interaction between hydrophobic side chains, and electrostatic repulsion between charged head groups all have roles in mediating the self-assembly of SLPs; the final self-assembled nanostructures are therefore dependent on their interplay. SLPs have shown diverse applications ranging from membrane protein stabilization and antimicrobial/anticancer agents to nanofabrication and biomineralization. Future advances in the self-assembly of SLPs will hinge on their large-scale production, the design of new functional SLPs with targeted properties, and the exploitation of new or improved applications.