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Antimicrobial peptides (AMPs) are a crucial part of the innate immune system of eukaryotes and present a possible alternative to common antibiotics. It is therefore of great importance to understand their modes of action. Using a single-molecule approach in combination with high resolution imaging and biofunctional assays we were able to determine the different steps occurring during the action of the α-helical AMP Sushi 1 during bacterial lysis in spatial and temporal resolution in a biologically relevant context. Furthermore, we comment on the use of Sushi 1 as a template for new peptides to learn more about structurefunction relationship of AMPs.