Interaction of a synthetic antimicrobial peptide with a model bilayer platform mimicking bacterial membranes

Lifang Niu, Thorsten Wohland, Wolfgang Knoll, Ingo Köper

    Research output: Contribution to journalArticle

    5 Citations (Scopus)

    Abstract

    Tethered bimolecular lipid membranes are solid supported membrane systems, which provide a versatile model platform for the study of many membrane related processes. Here, such an architecture has been used to study the interaction of the small synthetic antimicrobial peptide, V4, with membranes of various mixed lipid compositions, including membranes containing bacterial lipids. By investigating the binding of the peptide using a range of surface analytical techniques such as surface plasmon resonance and surface plasmon field-enhanced fluorescence spectroscopy as well as electrochemical impedance spectroscopy, a clear preference of the peptide for negatively charged membranes over zwitterionic ones has been shown. Additionally, the interactions seemed to indicate a cooperative behavior for the peptide binding to a membrane.

    Original languageEnglish
    Article number04E404
    JournalBiointerphases
    Volume12
    Issue number4
    DOIs
    Publication statusPublished - 1 Oct 2017

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