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- W4254093041 abstract "The mechanism of action of antimicrobial peptides is still not understood in molecular detail. Here, we present a molecular-dynamics and biophysical study of a cyclic antimicrobial peptide, c(KKLKKWKKLQ), and its inactive linear analogue. We establish that, relative to the linear peptide, the cyclic one binds stronger to negatively-charged membranes, folds at the interface and subsequently penetrates deeper into the bilayer. In the simulations, the cyclic peptide caused large perturbations in the bilayer and cooperatively opened a disordered toroidal pore, 1-2 nm in diameter. Electrophysiology measurements confirm discrete poration events of size 1.5-2 nm by the cyclic peptide. By employing dual-color fluorescence burst analysis, we show that both peptides are able to fuse/aggregate liposomes but only the cyclic peptide is able to form pores with a size of ∼2 nm. Fluorescence Resonance Energy Transfer (FRET) proved the fusiogenic activity of the cyclic versus the aggregation of vesicles caused by the linear peptide. The results provide detailed insight on the molecular basis of the activity of cyclic antimicrobial peptides." @default.
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- W4254093041 date "2011-02-01" @default.
- W4254093041 modified "2023-10-16" @default.
- W4254093041 title "The Molecular Basis for Antimicrobial Activity of Pore-Forming Cyclic Peptides" @default.
- W4254093041 doi "https://doi.org/10.1016/j.bpj.2010.12.2024" @default.
- W4254093041 hasPublicationYear "2011" @default.
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