Abstract
NATURALLY occurring membrane channels and pores are formed from a large family of diverse proteins, peptides and organic secon-dary metabolites whose vital biological functions include control of ion flow, signal transduction, molecular transport and produc-tion of cellular toxins. But despite the availability of a large amount of biochemical information about these molecules1, the design and synthesis of artificial systems that can mimic the bio-logical function of natural compounds remains a formidable task2–12. Here we present a simple strategy for the design of artifi-cial membrane ion channels based on a self-assembled cylindrical β-sheet peptide architecture13. Our systems—essentially stacks of peptide rings—display good channel-mediated ion-transport activ-ity with rates exceeding 107 ions s−1, rivalling the performance of many naturally occurring counterparts. Such molecular assemblies should find use in the design of novel cytotoxic agents, membrane transport vehicles and drug-delivery systems.
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Ghadiri, M., Granja, J. & Buehler, L. Artificial transmembrane ion channels from self-assembling peptide nanotubes. Nature 369, 301–304 (1994). https://doi.org/10.1038/369301a0
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DOI: https://doi.org/10.1038/369301a0
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