Abstract
Daptomycin is a cyclic lipopeptide of clinical importance in the treatment of multi-drug resistant infections, including those caused by methicillin-resistant S. aureus (MRSA) strains. Similar to other antimicrobial peptides, daptomycin binds with preference to the anionic cytoplasmic membranes typically found in prokaryotes. However, in contrast to most linear, alpha-helical peptides, daptomycin binds to lipid bilayers only in the presence of calcium ions and its activity is absolutely calcium-dependent. We measured the interaction of daptomycin with anionic lipid membranes using kinetic binding experiments and equilibrium titrations. The data were analyzed using an exact model describing the interactions of daptomycin with the lipid bilayer that includes solution and membrane-bound states, and the influence of calcium ions on daptomycin-lipid interactions. A preliminary version of the model was presented at the Biophysical Society Meeting in 2017. Here, we present a more complete analysis.
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