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Modular Design of Self-Assembling Peptide-Based Nanotubes

Research output: Contribution to journalArticle

Original languageEnglish
Pages (from-to)10554-10562
Number of pages9
JournalJournal of the American Chemical Society
Volume137
Issue number33
Early online date28 Jul 2015
DOIs
DateAccepted/In press - 28 Jul 2015
DateE-pub ahead of print - 28 Jul 2015
DatePublished (current) - 26 Aug 2015

Abstract

An ability to design peptide-based nanotubes (PNTs) rationally with defined and mutable internal channels would advance understanding of peptide self-assembly, and present new biomaterials for nanotechnology and medicine. PNTs have been made from Fmoc dipeptides, cyclic peptides, and lock-washer helical bundles. Here we show that blunt-ended α-helical barrels, that is, preassembled bundles of α-helices with central channels, can be used as building blocks for PNTs. This approach is general and systematic, and uses a set of de novo helical bundles as standards. One of these bundles, a hexameric α-helical barrel, assembles into highly ordered PNTs, for which we have determined a structure by combining cryo-transmission electron microscopy, X-ray fiber diffraction, and model building. The structure reveals that the overall symmetry of the peptide module plays a critical role in ripening and ordering of the supramolecular assembly. PNTs based on pentameric, hexameric, and heptameric α-helical barrels sequester hydrophobic dye within their lumens.

    Structured keywords

  • Bristol BioDesign Institute
  • BrisSynBio

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  • Full-text PDF (accepted author manuscript)

    Rights statement: This is the author accepted manuscript (AAM). The final published version (version of record) is available online via ACS at http://pubs.acs.org/doi/abs/10.1021/jacs.5b03973. Please refer to any applicable terms of use of the publisher.

    Accepted author manuscript, 1 MB, PDF document

    Licence: CC BY-NC

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