In proteins, chains of amino acids known as peptides are arranged in the form of an alpha helix. The peptides assemble into these helices because of the favourable formation of hydrogen bonds and other non-covalent interactions. Being able to control this self-assembly could open possible applications in tissue engineering, regenerative medicine and even organic semiconductors. 

In this study, published in Small, researchers designed a series of helical peptides and studied their self-assembly behaviour using a range of techniques, including neutron scattering. They were able to determine the effect of the different noncovalent interactions on the nanostructure formed. 

The system they have developed is a straightforward and versatile self-assembly method for creating complex biomolecules. As well as developing a system that could have applications in medicine, the work also provides a convenient approach for building biologically-inspired functional architectures for potential applications in functional materials and catalysis.​

Related publication: “Ordered Nanofibers Fabricated from Hierarchical Self-Assembling Processes of Designed α-Helical Peptides.” Small, 16, 45, 2003945 (2020) 

​DOI: 10.1002/smll.202003945

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