Format

Send to

Choose Destination
Nat Commun. 2014 Apr 7;5:3581. doi: 10.1038/ncomms4581.

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

Author information

1
1] Dipartimento di Scienze Chimiche Universit√° di Napoli 'Federico II' Complesso Universitario Monte S. Angelo Via Cynthia, 46, 80126 Napoli, Italia [2].
2
1] Department of Physics and Astronomy, University of Pennsylvania, 209 South 33rd Street, Philadelphia, Pennsylvania 19104-6396, USA [2] Department of Pharmaceutical Chemistry and the Cardiovascular Research Institute, University of California, CVRI-MC Box 3122, San Francisco, California 94158-9001, USA [3].
3
Dipartimento di Scienze Chimiche Universit√° di Napoli 'Federico II' Complesso Universitario Monte S. Angelo Via Cynthia, 46, 80126 Napoli, Italia.
4
Department of Pharmaceutical Chemistry and the Cardiovascular Research Institute, University of California, CVRI-MC Box 3122, San Francisco, California 94158-9001, USA.

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.

PMID:
24705140
PMCID:
PMC4013780
DOI:
10.1038/ncomms4581
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Nature Publishing Group Icon for PubMed Central
Loading ...
Support Center