ABSTRACT Ctxs are a family of α-helical, cationic, 3 kDa antibacterial peptides secreted by the female reproductive accessory glands of the Mediterranean fruit fly Ceratitis capitata. These peptides were found to display strong antibacterial activity and weak hemolytic activity. When reconstituted into planar lipid bilayers chemically synthesized Ctxs formed voltage-dependent ion channels according to the barrel-stave model. A synthetic truncated CtxA molecule resulted to permeabilize the outer and inner membranes of Escherichia coli cells.
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