4.8 Article

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

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NATURE COMMUNICATIONS
卷 5, 期 -, 页码 -

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NATURE PUBLISHING GROUP
DOI: 10.1038/ncomms4581

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  1. NIH [GM54616]
  2. Penn Nano/Bio Interface Center
  3. MRSEC program of NIH
  4. US Department of Energy, Office of Science, Office of Basic Energy Sciences [DE-AC02-06CH11357]
  5. LRSM at the University of Pennsylvania
  6. NSF [NSEC DMR-0425780]

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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.

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