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The linear gramicidins constitute a family of peptide antibiotics produced by the soil bacterium Bacillus brevis. The first antibiotics to be used in clinical practice, the linear gramicidins exert their antibacterial activity by forming bilayer-spanning channels that increase the monovalent cation permeability of target bacterial plasma membranes. Gramicidin channels are synthesized by non-ribosomal peptide synthesis on large protein complexes and contain both D- and L-amino acid residues; they were the first channels of known chemical composition to be studied. The channels effectively serve as cation-selective organic nanotubes that span lipid bilayer membranes and provide a basis for examining many aspects of ion-channel function and channel-lipid bilayer interactions. The nanotube properties can be tuned by means of mutations or chemical changes to the subunit architecture, as well as by altering the channels’ bilayer environment (e.g., the bilayer thickness). Indeed, many analogue sequences within the extended peptide family have been prepared by semi-synthesis or total synthesis. Diverse applications of gramicidin channels have enhanced our understanding of the microphysics of ion permeation, lipid-protein interactions and membrane protein function.