Peptides are chains of amino acids, the building blocks of proteins. They are involved in a variety of biological processes, including cell signaling, hormone regulation, and immune response. In recent years, there has been growing interest in the use of peptides for therapeutic purposes. However, the ability to design peptides with specific properties has been limited by our understanding of how peptides self-assemble.

A team of researchers at the University of California, San Diego, has now made a significant breakthrough in this area. They have discovered a novel, ordered assembly of alternating peptides, and they have identified the driving forces behind this assembly.

The researchers used a combination of experimental and computational techniques to study the self-assembly of two different peptides. They found that the peptides formed alternating layers, with each layer consisting of one type of peptide. The layers were stacked in a regular, repeating pattern, creating a highly ordered structure.

The researchers were able to identify two key factors that drove the formation of this ordered assembly. First, the peptides had opposite charges, which allowed them to electrostatically attract each other. Second, the peptides had complementary shapes, which allowed them to fit together like puzzle pieces.

The researchers believe that their findings could have important implications for the design of peptide-based therapeutics. By understanding the forces that drive peptide self-assembly, scientists may be able to design peptides that self-assemble into specific structures with desired properties. This could lead to the development of new drugs and treatments for a variety of diseases.

The study was published in the journal Nature Communications.