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

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 Commun

journal_title

Nature communications

authors

Pavone V,Zhang SQ,Merlino A,Lombardi A,Wu Y,DeGrado WF

doi

10.1038/ncomms4581

subject

Has Abstract

pub_date

2014-04-07 00:00:00

pages

3581

issn

2041-1723

pii

ncomms4581

journal_volume

5

pub_type

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