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: 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 led by Ivan Huc, a professor in the Department of Chemistry and Pharmacy at LMU, have teamed up with colleagues from Berlin, Bordeaux and Nantes to develop an artificial protein–foldamer pair that meets this requirement.
"A specifically selected protein recognizes a synthetic molecule and binds to it with high affinity," Huc summarizes. "The sizeable contact surface, which has a clearly defined structure, makes it possible to use the complex as a modular building block for larger molecular architectures." The team has now presented the results in the journal Nature Chemistry. This new paper focuses on what is known as a foldamer, an artificial molecule that, like a protein, folds into a stable shape—in this case, a helix.
The researchers were looking for a protein that would be the right counterpart for this foldamer. In their research, they used ribosome display, a biochemical method that identifies protein–protein interactions among hundreds of billions of different protein variants and proved effective for foldamer–protein interactions as well. After four rounds of selection, the team identified variant C10 of a protein scaffold known as Nanofitin.
The right-handed P-helix of the foldamer binds C10 with great strength, whereas no binding was detected for the left-handed M-helix. The protein and foldamer are in contact with each other over a large, clearly defined area. Previous protein–foldamer complexes were less stable or required flexible connectors.
The team investigated how the protein and foldamer fit together structurally using nuclear magnetic resonance (NMR) spectroscopy and X-ray crystallography, among other techniques. The researchers also analyzed larger complexes using mass spectrometry. They then used these binding pairs to create more complex structures.
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