This article has been reviewed according to Science X's editorial process and policies. Editors have highlighted the following attributes while ensuring the content's credibility: Honeycomb-shaped structures are familiar from beehives. Researchers have now designed molecules that self-assemble into a similar pattern on a scale far too small to see with the naked eye.
These molecules are peptides: short chains of amino acids, the building blocks of proteins. Each peptide consists of only nine amino acids. Many identical copies assemble into tiny fibers with a honeycomb-like interior filled with water.
The Max Planck Institute for Polymer Research, the University of Ulm and Ulm University Hospital are involved in the work. The study, with co-first authors Jasmina Gačanin and Francesca Mazzotta, has been published in Nature. "The molecules come with their own assembly instructions," says Tanja Weil, director at the Max Planck Institute for Polymer Research, who led the study with her colleague Katharina Landfester.
"The crucial step is to understand how such a short peptide sequence gives rise to a much larger, ordered structure." The researchers designed a short peptide sequence of nine amino acids and studied it in several variants. They found that this amino acid sequence dictates how the peptides arrange themselves. Two peptides pair up, and three meet at each junction.
This creates hexagonal rings that join side by side into a honeycomb and stack along the fiber. The resulting fibers have many parallel, continuous channels about five nanometers across. By systematically substituting individual segments in the amino acid sequence, the researchers determined which segments are necessary for a honeycomb structure to form.
To do this, they used a special type of electron microscopy known as cryo-electron microscopy. In this technique, the sample is flash-frozen in a thin layer of ice and imaged in its natural, hydrated state. This allows scientists to determine exactly how neighboring peptides interlock.
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