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    Unveiling the binding and orientation of the antimicrobial peptide Plantaricin 149 in zwitterionic and negatively charged membranes

    Kumagai, P.S. and Sousa, V.K. and Donato, M. and Itri, R. and Beltramini, L.M. and Araujo, A.P.U. and Buerck, J. and Wallace, Bonnie and Lopes, J.L.S. (2019) Unveiling the binding and orientation of the antimicrobial peptide Plantaricin 149 in zwitterionic and negatively charged membranes. European Biophysics Journal , ISSN 0175-7571. (In Press)

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    Abstract

    Antimicrobial peptides are a large group of natural compounds which present promising properties for the pharmaceutical and food industries, such as broad-spectrum activity, potential for use as natural preservatives, and reduced propensity for development of bacterial resistance. Plantaricin 149 (Pln149), isolated from Lactobacillus plantarum NRIC 149, is a peptide with the ability to inhibit bacteria from the Listeria and Staphylococcus genera, which is capable of promoting inhibition and disruption of yeast cells. In this study, the interactions of Pln149 with model membranes composed of zwitterionic and/or anionic phospholipids were investigated using a range of biophysical techniques, including isothermal titration calorimetry, surface tension measurements, synchrotron radiation circular dichroism spectroscopy, oriented circular dichroism spectroscopy, and optical microscopy, in order to elucidate their mode of interactions and provide insight into their functional roles. In anionic model membranes, the binding of Pln149 to lipid bilayers is an endothermic process and induces a helical secondary structure in the peptide. The helices bind parallel to the surfaces of lipid bilayers and can promote vesicle disruption, depending on peptide concentration. Although Pln149 has relatively low affinity for zwitterionic liposomes, it is able to adsorb at their lipid interfaces, disturbing the lipid packing, assuming a similar parallel helix structure with a surface-bound orientation, and promoting an increase in the membrane surface area. Such findings can explain the intriguing inhibitory action of Pln149 in yeast cells whose cell membranes have a significant zwitterionic lipid composition.

    Metadata

    Item Type: Article
    Additional Information: The final publication is available at Springer via the link above.
    Keyword(s) / Subject(s): antimicrobial peptide, oriented circular dichroism spectroscopy, mechanism of action, peptide-lipid interactions, synchrotron radiation circular dichroism spectroscopy
    School: Birkbeck Schools and Departments > School of Science > Biological Sciences
    Depositing User: Administrator
    Date Deposited: 03 Jul 2019 08:54
    Last Modified: 26 Sep 2019 23:18
    URI: http://eprints.bbk.ac.uk/id/eprint/28003

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