Crystal structure of an amphiphilic foldamer reveals a 48-mer assembly comprising a hollow truncated octahedron.
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.
1] Dipartimento di Scienze Chimiche Universitá di Napoli 'Federico II' Complesso Universitario Monte S. Angelo Via Cynthia, 46, 80126 Napoli, Italia [2].
Vincenzo
V
Pavone
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].
Shao-Qing
SQ
Zhang
Dipartimento di Scienze Chimiche Universitá di Napoli 'Federico II' Complesso Universitario Monte S. Angelo Via Cynthia, 46, 80126 Napoli, Italia.
Antonello
A
Merlino
Dipartimento di Scienze Chimiche Universitá di Napoli 'Federico II' Complesso Universitario Monte S. Angelo Via Cynthia, 46, 80126 Napoli, Italia.
Angela
A
Lombardi
Department of Pharmaceutical Chemistry and the Cardiovascular Research Institute, University of California, CVRI-MC Box 3122, San Francisco, California 94158-9001, USA.
Yibing
Y
Wu
Department of Pharmaceutical Chemistry and the Cardiovascular Research Institute, University of California, CVRI-MC Box 3122, San Francisco, California 94158-9001, USA.
William F
WF
DeGrado
D006860:Hydrogen Bonding; D011108:Polymers / Q000737:chemistry*; D017510:Protein Folding; D017433:Protein Structure, Secondary
D011108:Polymers