Berkeley Lab scientists have developed a nanoscale rope that braids itself, as seen in this atomic force microscopy image of the structure at a resolution of one-millionth of a meter.
Scientists at the U.S. Department of Energy’s Lawrence Berkeley National Laboratory (Berkeley Lab) have coaxed polymers to braid themselves into wispy nanoscale ropes that approach the structural complexity of biological materials.
The aqueous self-assembly of a sequence-specific bioinspired peptoid diblock copolymer into monodisperse superhelices is demonstrated to be the result of a hierarchical process, strongly dependent on the charging level of the molecule. The partially charged amphiphilic diblock copolypeptoid, forms superhelices in high yields, with diameters of 624 ± 69 nm and lengths ranging from 2 to 20 μm. Chemical analogs coupled with X-ray scattering and crystallography of a model compound have been used to develop a hierarchical model of self-assembly. Lamellar stacks roll up to form a supramolecular double helical structure with the internal ordering of the stacks being mediated by crystalline aromatic side chain−side chain interactions within the hydrophobic block. The role of electrostatic and hydrogen bonding interactions in the hydrophilic block is also investigated and found to be important in the self-assembly process.
The scientists created the conditions for synthetic polymers called polypeptoids to assemble themselves into ever more complicated structures: first into sheets, then into stacks of sheets, which in turn roll up into double helices that resemble a rope measuring only 600 nanometers in diameter (a nanometer is a billionth of a meter).
“This hierarchichal self assembly is the hallmark of biological materials such as collagen, but designing synthetic structures that do this has been a major challenge,” says Ron Zuckermann, who is the Facility Director of the Biological Nanostructures Facility in Berkeley Lab’s Molecular Foundry.
In addition, unlike normal polymers, the scientists can control the atom-by-atom makeup of the ropy structures. They can also engineer helices of specific lengths and sequences. This “tunability” opens the door for the development of synthetic structures that mimic biological materials’ ability to carry out incredible feats of precision, such as homing in on specific molecules.
The scientists worked with chains of bioinspired polymers called a peptoids. Peptoids are structures that mimic peptides, which nature uses to form proteins, the workhorses of biology. Instead of using peptides to build proteins, however, the scientists are striving to use peptoids to build synthetic structures that behave like proteins.
The team started with a block copolymer, which is a polymer composed of two or more different monomers.
“Simple block copolymers self assemble into nanoscale structures, but we wanted to see how the detailed sequence and functionality of bioinspired units could be used to make more complicated structures,” says Rachel Segalman, a faculty scientist at Berkeley Lab and professor of Chemical and Biomolecular Engineering at University of California, Berkeley.
With this in mind, the peptoid pieces were robotically synthesized, processed, and then added to a solution that fosters self assembly.
The result was a variety of self-made shapes and structures, with the braided helices being the most intriguing. The hierarchical structure of the helix, and its ability to be manipulated atom-by-atom, means that it could be used as a template for mineralizing complex structures on a nanometer scale.
“The idea is to assemble structurally complex structures at the nanometer scale with minimal input,” says Hannah Murnen. She adds that the scientists next hope is to capitalize on the fact that they have minute control over the structure’s sequence, and explore how very small chemical changes alter the helical structure.
Says Zuckermann, “These braided helices are one of the first forays into making atomically defined block copolymers. The idea is to take something we normally think of as plastic, and enable it to adopt structures that are more complex and capable of higher function, such as molecular recognition, which is what proteins do really well.”
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