Foldamer–protein pair unlocks precise building blocks for artificial molecular materials
Proteins form complex three-dimensional shapes and can join together to create larger structures. Researchers want to use these properties to make artificial materials. However, arranging proteins and synthetic molecules together with a high level of structural precision is no easy task. This is partly because of the lack of large, clearly defined contact surfaces between the two components.
Researchers at LMU have teamed up with colleagues from Berlin, Bordeaux, and Nantes to develop an artificial protein-foldamer pair that forms a strong, defined contact surface for creating precise, modular building blocks in artificial molecular materials. Foldamers are artificial molecules that fold into stable shapes, similar to proteins.
The team used a method called ribosome display to identify a suitable protein partner. After four rounds of selection, they found variant C10 of the protein scaffold Nanofitin, which binds the foldamer with great strength. The right-handed P-helix of the foldamer pairs with C10, while the left-handed M-helix does not bind. This protein-foldamer pair forms a large, clearly defined contact area, making it a stable building block.
The researchers used techniques like nuclear magnetic resonance (NMR) spectroscopy and X-ray crystallography to analyze the structural fit between the protein and foldamer. They also created larger complexes and intricate structures using these binding pairs. The arrangement of these building blocks can be controlled by their geometry, allowing for the creation of one-dimensional zigzag-shaped networks and other complex structures.
The foldamer's length influences the spacing and orientation of bound proteins, and crystal lattices formed by these structures exhibit high porosity, with potential cavities large enough to accommodate nanoparticles or large molecules with a diameter of about 5 nanometers. This discovery opens up possibilities for using artificial foldamers as precise connectors in protein architectures, potentially leading to the creation of porous three-dimensional materials and introducing functional groups into such structures.
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