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Investigating Effects and Determinants of PAP248–286‐Membrane Interactions: Membrane Leakage and Peptide/Lipid Co‐Aggregation

Many amyloid‐forming peptides appear to possess potentially beneficial antimicrobial activities. Furthermore, it has been suggested that this previously unrecognized activity may have a role in innate immunity. Antimicrobial peptides, which are important effectors in the innate immune response, can act either directly by inducing membrane leakage and cytolysis, or indirectly through bacterial adhesion inhibition or enhanced phagocytosis via bacterial agglutination. Amyloid‐forming peptides themselves display a variety of membrane‐disrupting and membrane‐remodeling activities, including membrane leakage and vesicle aggregation. In turn, some membranes are known to catalyze amyloid formation. Peptide‐membrane interactions may thus underlie both the pathological activity of amyloid‐forming peptides through their cytotoxicity due to pre‐fibrillar oligomers and their beneficial functions through their direct or indirect antimicrobial activities. Therefore, studying the factors driving the interactions between amyloid‐forming peptides and membranes may be valuable in understanding their roles in both healthy and diseased states.