Recent advances in the development and application of peptide self-assemblies in infection control

Peptide self-assemblies display distinct physical and structural transitions, ranging from the early small assemblies, or oligomers, to long nanosheets, nanobelts, nanotubes, and nanofibers formed into distinct hydrogels. Because of changes in charge distribution and protection of cleavage sites, self-assembled peptides can have high resistance to enzymatic degradation. As potential candidates for biomedical applications, it is important to understand how peptides self-assemble and how the processes can be manipulated. Following the diverse approaches recently reported to control their assembling processes, many de novo-designed short peptides can be applied to infection control in various conditions, such as nanocarriers in drug delivery, wound dressings, and postsurgery antimicrobial/antiviral spreads and coatings. Here we present an overview of recent advances in peptide self-assembly mechanisms and the relationship between self-assembly behaviors and their infection-combatting effects. At the end of this review, concluding remarks and future perspectives are provided.