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

Vincenzo Pavone (), Shao-Qing Zhang, Antonello Merlino, Angela Lombardi, Yibing Wu () and William F. DeGrado ()
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Vincenzo Pavone: 46
Shao-Qing Zhang: University of Pennsylvania
Antonello Merlino: 46
Angela Lombardi: 46
Yibing Wu: University of California
William F. DeGrado: University of California

Nature Communications, 2014, vol. 5, issue 1, 1-7

Abstract: 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.

Date: 2014
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms4581

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DOI: 10.1038/ncomms4581

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