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|Title:||Modulating charge-dependent and folding-mediated antimicrobial interactions at peptide–lipid interfaces|
|Authors:||IAVICOLI PATRIZIA; ROSSI FRANCOIS; LAMARRE BAPTISTE; BELLA ANGELO; RYADNOV MAXIM; CALZOLAI LUIGI|
|Citation:||EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS vol. 46 no. 4 p. 375-382|
|Type:||Articles in periodicals and books|
|Abstract:||Peptide-lipid interactions support a variety of biological functions. Of particular interest are 19 those that underpin fundamental mechanisms of innate immunity that are programmed in host 20 defense or antimicrobial peptide sequences found virtually in all multicellular organisms. Here 21 we synthetically modulate antimicrobial peptide-lipid interactions using an archetypal helical 22 antimicrobial peptide and synthetic membranes mimicking bacterial and mammalian membranes 23 in solution. We probe these interactions as a function of membrane-induced folding, membrane 24 stability and peptide-lipid ratios using a correlative approach encompassing light scattering and 25 spectroscopy measurements. The peptide behavior is assessed against that of its anionic 26 counterpart. The results obtained indicate strong correlations between peptide folding and 27 membrane type supporting folding-responsive binding of antimicrobial peptides to bacterial 28 membranes. The study provides a straightforward approach for modulating structure-activity 29 relationships in the context of membrane-induced antimicrobial action thus holding promise for 30 the rational design of potent antimicrobial agents.|
|JRC Directorate:||Health, Consumers and Reference Materials|
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