Structure and function of lipopeptide antibiotics and of CAMP factor, a bacterial pore-forming toxin

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The proposed research concerns the mode of action of a medically important antibiotic, daptomycin, as well as the two related lipopeptide antibiotics A54145D and CDA. These antibiotics kill bacteria by attacking and permeabilizing their cell membranes. We will explore the exact nature of this mode of action with biochemical and biophysical methods and define the correlations between function and molecular structure. This will provide useful information for future efforts to modify and improve antimicrobial activity. A second research area included in this proposal concerns a protein toxin produced by a pathogenic bacterium, Streptococcus agalactiae. This toxin, CAMP factor, also damages cell membranes, but in this case the target cell membranes of those of human cells. We will investigate the structure of the toxin-mediated membrane lesion with biochemical and fluorescence methods.