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Modular Design of Self-Assembling Peptide-Based Nanotubes

DOI: 10.1021/jacs.5b03973 DOI Help

Authors: Natasha Burgess (University of Bristol) , Thomas H. Sharp (Leiden University Medical Center) , Franziska Thomas (University of Bristol) , Christopher W. Wood (University of Bristol) , Andrew Thomson (University of Bristol) , Nathan Zaccai (University of Bristol) , Leo Brady (University of Bristol) , Louise Serpell (University of Sussex) , Derek N. Woolfson (University of Bristol)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Journal Of The American Chemical Society , VOL 137 (33)

State: Published (Approved)
Published: August 2015
Diamond Proposal Number(s): 8922

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.

Subject Areas: Biology and Bio-materials


Instruments: I03-Macromolecular Crystallography , I04-Macromolecular Crystallography

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