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.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Pavone V,Zhang SQ,Merlino A,Lombardi A,Wu Y,DeGrado WFdoi
10.1038/ncomms4581subject
Has Abstractpub_date
2014-04-07 00:00:00pages
3581issn
2041-1723pii
ncomms4581journal_volume
5pub_type
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