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Issue 40, 2013
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Self-assembly of three bacterially-derived bioactive lipopeptides

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Abstract

The self-assembly in aqueous solution of three lipopeptides obtained from Bacillus subtilis has been investigated. The lipopeptides surfactin, plipastatin and mycosubtilin contain distinct cyclic peptide headgroups as well as differences in alkyl chain length, branching and chain length distribution. Cryogenic transmission electron microscopy and X-ray scattering reveal that surfactin and plipastatin aggregate into 2 nm-radius spherical micelles, whereas in complete contrast mycosubtilin self-assembles into extended nanotapes based on bilayer ordering of the lipopeptides. Circular dichroism and FTIR spectroscopy indicate the presence of turn structures in the cyclic peptide headgroup. The unexpected distinct mode of self-assembly of mycosubtilin compared to the other two lipopeptides is ascribed to differences in the surfactant packing parameter. This in turn is due to specific features of the conformation of the peptide headgroup and alkyl chain branching.

Graphical abstract: Self-assembly of three bacterially-derived bioactive lipopeptides

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Publication details

The article was received on 30 May 2013, accepted on 21 Aug 2013 and first published on 21 Aug 2013


Article type: Paper
DOI: 10.1039/C3SM51514A
Citation: Soft Matter, 2013,9, 9572-9578
  • Open access: Creative Commons BY license
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    Self-assembly of three bacterially-derived bioactive lipopeptides

    I. W. Hamley, A. Dehsorkhi, P. Jauregi, J. Seitsonen, J. Ruokolainen, F. Coutte, G. Chataigné and P. Jacques, Soft Matter, 2013, 9, 9572
    DOI: 10.1039/C3SM51514A

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