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Dynamic transition of α-helix to β-sheet structure in linear surfactin correlating to critical micelle concentration

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Summary

Linear heptapeptide surfactin was prepared by alkaline cleavage of the lactone ring of cyclic surfactin. The structure of linear surfactin was characterised and confirmed by FAB-mass-spectroscopy, FT-IR and HPLC analysis. It was found that linear surfactin easily forms micelles in aqueous solutions by coordinating β-sheet formation from α-helical monomolecules, and the cmc value found to be 1.28×10−5 M. The CD spectra indicates conformational change of linear surfactin from α-helical below cmc to β-sheet above cmc.

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Authors and Affiliations

  1. National Institute of Materials and Chemical Research, Ibaraki305, Tsukuba, Japan

    Mohamad Osman, Yutaka Ishigami & Keiichiro Ishikawa

  2. National Institute of Life Science and Human Technology, Ibaraki305, Tsukuba, Japan

    Yasuko Ishizuka

  3. Department of Biochemistry and Molecular Biology, University of Bergen, Årstadveien 19, N-5009, Bergen, Norway

    Holm Holmsen

Authors
  1. Mohamad Osman
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  2. Yutaka Ishigami
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  3. Keiichiro Ishikawa
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  4. Yasuko Ishizuka
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  5. Holm Holmsen
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Osman, M., Ishigami, Y., Ishikawa, K. et al. Dynamic transition of α-helix to β-sheet structure in linear surfactin correlating to critical micelle concentration. Biotechnol Lett 16, 913–918 (1994). https://doi.org/10.1007/BF00128624

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  • DOI: https://doi.org/10.1007/BF00128624

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