Abstract
Proteins can readily assemble into rigid, crystalline and functional structures such as viral capsids and bacterial compartments. Despite ongoing advances, it is still a fundamental challenge to design and synthesize protein-mimetic molecules to form crystalline structures. Here we report the lattice self-assembly of cyclodextrin complexes into a variety of capsid-like structures such as lamellae, helical tubes and hollow rhombic dodecahedra. The dodecahedral morphology has not hitherto been observed in self-assembly systems. The tubes can spontaneously encapsulate colloidal particles and liposomes. The dodecahedra and tubes are respectively comparable to and much larger than the largest known virus. In particular, the resemblance to protein assemblies is not limited to morphology but extends to structural rigidity and crystallinity—a well-defined, 2D rhombic lattice of molecular arrangement is strikingly universal for all the observed structures. We propose a simple design rule for the current lattice self-assembly, potentially opening doors for new protein-mimetic materials.
Highlights
Proteins can readily assemble into rigid, crystalline and functional structures such as viral capsids and bacterial compartments
All living organisms are self-assembled entities where two major kinds of self-assembly are involved: the assembly of lipids into soft, fluidic membranes mainly driven by the hydrophobic interaction and the assembly of proteins into rigid, crystalline structures driven by a combination of hydrophobic, H-bonding and electrostatic interactions[1,2,3,4,5,6,7,8,9,10,11,12]
We reveal the existence of another structure, hollow rhombic dodecahedra and, more importantly, scrutinize the system on the microscopic/molecular scale to identify a high structural rigidity and well-defined, in-plane crystallinity
Summary
Proteins can readily assemble into rigid, crystalline and functional structures such as viral capsids and bacterial compartments. We report the lattice self-assembly of cyclodextrin complexes into a variety of capsidlike structures such as lamellae, helical tubes and hollow rhombic dodecahedra. The properties and functions of carbon allotropes, lipid assemblies and protein assemblies are, drastically different as carbon atoms are connected by chemical bonds, lipids by hydrophobic interactions and proteins by a combination of intermolecular interactions. In this context, what has been gradually recognized is the importance of intermolecular interactions, structural flexibility/rigidity and fluidity/crystallinity over that of morphology. We reveal the existence of another structure, hollow rhombic dodecahedra and, more importantly, scrutinize the system on the microscopic/molecular scale to identify a high structural rigidity and well-defined, in-plane crystallinity
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