Title: Modulating charge-dependent and folding-mediated antimicrobial interactions at peptide–lipid interfaces
Authors: IAVICOLI PATRIZIAROSSI FRANCOISLAMARRE BAPTISTEBELLA ANGELORYADNOV MAXIMCALZOLAI LUIGI
Citation: EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS vol. 46 no. 4 p. 375-382
Publisher: SPRINGER
Publication Year: 2017
JRC N°: JRC93108
ISSN: 0175-7571
URI: http://publications.jrc.ec.europa.eu/repository/handle/JRC93108
DOI: 10.1007/s00249-016-1180-8
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

Files in This Item:
There are no files associated with this item.


Items in repository are protected by copyright, with all rights reserved, unless otherwise indicated.