Influence of self-assembly on the performance of antimicrobial peptides

With a rapidly growing number of bacterial strains displaying resistance against conventional antibiotics, the development of novel types of antimicrobial agents represents an important health challenge. Antimicrobial peptides (AMPs) has attracted interest in this context, as these can be designed to display potent broad-spectrum antimicrobial as well as antiinflammatory effects, but simultaneously low toxicity against human cells. Much of the work on AMPs has been focused on membrane interactions of monomeric AMPs, and how these can be controlled by peptide design to obtain selective disruption of bacterial membranes. However, a growing body of research has demonstrated that AMPs offer opportunities as antimicrobials beyond this through their self-assembly. An overview is therefore provided of the current understanding of the interplay between AMP aggregation and antimicrobial effects, including the role of oligomerization and self-assembly on membrane interactions and antimicrobial effects, AMP interactions with amyloid-forming peptides/proteins, AMP self assemblies as antimicrobial biomaterials, and AMP-induced flocculation of bacteria and bacterial lipopolysaccharides as a novel pathway for confinement of infection and inflammation.