Crystal structure of an amphiphilic foldamer reveals a 48-mer assembly comprising a hollow truncated octahedron.
Publication Type:Journal Article
Source:Nat Commun, Volume 5, p.3581 (2014)
Keywords:Hydrogen Bonding, Polymers, Protein Folding, Protein Structure, Secondary
<p>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.</p>