De novo protein design is a powerful tool for preparing small proteins with desired folds and functions. In this work, David Baker and colleagues report a combined computational and experimental approach to designing and screening folded mini-proteins, consisting of around 40 residues, to bind and target influenza haemagglutinin, a protein on the surface of the flu virus, and botulinum neurotoxin B, a cause of botulism. This high-throughput method produces binding proteins that are more stable and much smaller than traditional antibody therapies, that can be readily modulated and that elicit very little immune response. The optimal haemagglutinin binders show protection against influenza infection in vivo, illustrating the potential of this method for antiviral and other therapeutic applications.
- Massively parallel de novo protein design for targeted therapeutics (Article p74, doi: 10.1038/nature23912)
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