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Conclusions

In conclusion, although within limited ranges of concentration and applied voltage, we have shown that the assembly of the alamethicin molecules was successfully modulated by the extramembrane leucine zipper sequence. As the assembly was modulated, ionselectivity of the channel became prominent. We have also shed light on the effect of the bulkiness of the extramembrane segments on the assembly modulation. The results obtained in this study should provide useful information on the development of artificial sensors and receptors.

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© 2002 Kluwer Academic Publishers

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Futaki, S. (2002). Assembly Modulation of Channel-Forming Peptides. In: Self-Assembling Peptide Systems in Biology, Medicine and Engineering. Springer, Dordrecht. https://doi.org/10.1007/0-306-46890-5_7

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  • DOI: https://doi.org/10.1007/0-306-46890-5_7

  • Publisher Name: Springer, Dordrecht

  • Print ISBN: 978-0-7923-7090-1

  • Online ISBN: 978-0-306-46890-2

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