Abstract
Antimicrobial peptides and pore-forming toxins are important effectors in innate immune defence reactions. But their mode of action, comprising the insertion into cholesterol-containing membranes is not known. Here we explore the mechanical implications of pore-formation by extracellular protein assemblies that drive cellular uptake reactions by leverage-mediated (LM) processes, where oligomeric adhesion molecules bent membrane-receptors around ‘hinge’-like lipophorin particles. The interactions of antimicrobial peptides, pore-forming toxins and biologically active proteins with LMassemblies provide a new paradigm for the configurational specificity and sterical selectivity of biologically active peptides.