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Antimicrobial peptides and pore-forming toxins are important effectors in innate immune defencereactions. But their mode of action, comprising the insertion into cholesterol-containing membranes isnot known. Here we explore the mechanical implications of pore-formation by extracellular proteinassemblies that drive cellular uptake reactions by leverage-mediated (LM) processes, whereoligomeric adhesion molecules bent membrane-receptors around ‘hinge’-like lipophorin particles. Theinteractions of antimicrobial peptides, pore-forming toxins and biologically active proteins with LMassembliesprovide a new paradigm for the configurational specificity and sterical selectivity ofbiologically active peptides.