The browser you are using is not supported by this website. All versions of Internet Explorer are no longer supported, either by us or Microsoft (read more here: https://www.microsoft.com/en-us/microsoft-365/windows/end-of-ie-support).

Please use a modern browser to fully experience our website, such as the newest versions of Edge, Chrome, Firefox or Safari etc.

Portrait of Tommy Nylander. Photo: Kennet Ruona

Tommy Nylander

Professor

Portrait of Tommy Nylander. Photo: Kennet Ruona

Effect of fengycin, a lipopeptide produced by Bacillus subtilis, on model biomembranes

Author

  • Magali Deleu
  • Michel Paquot
  • Tommy Nylander

Summary, in English

Fengycin is a biologically active lipopeptide produced by several Bacillus subtilis strains. The lipopeptide is known to develop antifungal activity against filamentous fungi and to have hemolytic activity 40-fold lower than that of surfactin, another lipopeptide produced by B. subtilis. The aim of this work is to use complementary biophysical techniques to reveal the mechanism of membrane perturbation by fengycin. These include: 1), the Langmuir trough technique in combination with Brewster angle microscopy to study the lipopeptide penetration into monolayers; 2), ellipsometry to investigate the adsorption of fengycin onto supported lipid bilayers; 3), differential scanning calorimetry to determine the thermotropic properties of lipid bilayers in the presence of fengycin; and 4), cryogenic transmission electron microscopy, which provides information on the structural organization of the lipid/lipopeptide system. From these experiments, the mechanism of fengycin action appears to be based on a two-state transition controlled by the lipopeptide concentration. One state is the monomeric, not deeply anchored and nonperturbing lipopeptide, and the other state is a buried, aggregated form, which is responsible for membrane leakage and bioactivity. The mechanism, thus, appears to be driven mainly by the physicochemical properties of the lipopeptide, i.e., its amphiphilic character and affinity for lipid bilayers.

Department/s

  • Physical Chemistry

Publishing year

2008

Language

English

Pages

2667-2679

Publication/Series

Biophysical Journal

Volume

94

Issue

7

Document type

Journal article

Publisher

Cell Press

Topic

  • Biophysics

Status

Published

ISBN/ISSN/Other

  • ISSN: 1542-0086