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Crystal structure of an amphiphilic foldamer reveals a 48-mer assembly comprising a hollow truncated octahedron

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  • Vincenzo Pavone
  • Shao-Qing Zhang

    (University of Pennsylvania
    University of California)

  • Antonello Merlino
  • Angela Lombardi
  • Yibing Wu

    (University of California)

  • William F. DeGrado

    (University of California)

Abstract

Foldamers provide an attractive medium to test the mechanisms by which biological macromolecules fold into complex three-dimensional structures, and ultimately to design novel protein-like architectures with properties unprecedented in nature. Here, we describe a large cage-like structure formed from an amphiphilic arylamide foldamer crystallized from aqueous solution. Forty-eight copies of the foldamer assemble into a 5-nm cage-like structure, an omnitruncated octahedron filled with well-ordered ice-like water molecules. The assembly is stabilized by a mix of arylamide stacking interaction, hydrogen bonding and hydrophobic forces. The omnitruncated octahedra tessellate to form a cubic crystal. These findings may provide an important step towards the design of nanostructured particles resembling spherical viruses.

Suggested Citation

  • Vincenzo Pavone & Shao-Qing Zhang & Antonello Merlino & Angela Lombardi & Yibing Wu & William F. DeGrado, 2014. "Crystal structure of an amphiphilic foldamer reveals a 48-mer assembly comprising a hollow truncated octahedron," Nature Communications, Nature, vol. 5(1), pages 1-7, May.
    • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms4581
    DOI: 10.1038/ncomms4581
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