This study describes a new in silico method for designing ligand-binding proteins. The technique involved computationally generating potential binding proteins from protein scaffolds, followed by iterative in vitro screening to optimize binding affinity. Using this method, the authors generated proteins that bound to the steroid digoxigenin with picomolar affinity and high selectivity over related steroids. The authors note that this method could be useful for creating therapeutic scavengers and binding domains for diagnostics.
References
Tinberg, C. E. et al. Computational design of ligand-binding proteins with high affinity and selectivity. Nature 501, 212–216 (2013)
Rights and permissions
About this article
Cite this article
Harrison, C. Designing optimal ligand-binding proteins. Nat Rev Drug Discov 12, 742 (2013). https://doi.org/10.1038/nrd4141
Published:
Issue Date:
DOI: https://doi.org/10.1038/nrd4141