ArticlePloS one2013
Selection of specific protein binders for pre-defined targets from an optimized library of artificial helicoidal repeat proteins (alphaRep).
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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21 citing papers in PubMed.
- Structural determination of small proteins by cryo-EM using a coiled coil module strategy.Scientific reports · 2025Article
- Chameleon sequences-Structural effects.PloS one · 2025Article
- Sterile inflammation induces vasculopathy and chronic lung injury in murine sickle cell disease.Free radical biology & medicine · 2024Article
- Design, synthesis, and characterization of protein origami based on self-assembly of a brick and staple artificial protein pair.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Design of an artificial phage-display library based on a new scaffold improved for average stability of the randomized proteins.Scientific reports · 2023Article
- Programmable DARPin-based receptors for the detection of thrombotic markers.Nature chemical biology · 2022Article
- Biosynthetic proteins targeting the SARS-CoV-2 spike as anti-virals.PLoS pathogens · 2022Article
- Macromolecular interactions in vitro, comparing classical and novel approaches.European biophysics journal : EBJ · 2021Article
- Occupation of a thermoresistant-scaffold (αRep) at SP1-NC cleavage site disturbs the function of HIV-1 protease.Bioscience reports · 2020Article
- Protein-Catalyzed Capture Agents.Chemical reviews · 2019Review
- Insight into microtubule nucleation from tubulin-capping proteins.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Selection and Characterization of Artificial Proteins Targeting the Tubulin α Subunit.Structure (London, England : 1993) · 2019Article
- Ligand-induced conformational switch in an artificial bidomain protein scaffold.Scientific reports · 2019Article
- Article
- A Modular Receptor Platform To Expand the Sensing Repertoire of Bacteria.ACS synthetic biology · 2018Article
- Structural Analysis of the Hanks-Type Protein Kinase YabT FromFrontiers in microbiology · 2018Article
- Alpha-helicoidal HEAT-like Repeat Proteins (αRep) Selected as Interactors of HIV-1 Nucleocapsid Negatively Interfere with Viral Genome Packaging and Virus Maturation.Scientific reports · 2017Article
- Design and applications of a clamp for Green Fluorescent Protein with picomolar affinity.Scientific reports · 2017Article
- Specific GFP-binding artificial proteins (αRep): a new tool for in vitro to live cell applications.Bioscience reports · 2015Article
- Amphipol-mediated screening of molecular orthoses specific for membrane protein targets.The Journal of membrane biology · 2014Article
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9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We previously designed a new family of artificial proteins named αRep based on a subgroup of thermostable helicoidal HEAT-like repeats. We have now assembled a large optimized αRep library. In this library, the side chains at each variable position are not fully randomized but instead encoded by a distribution of codons based on the natural frequency of side chains of the natural repeats family. The library construction is based on a polymerization of micro-genes and therefore results in a distribution of proteins with a variable number of repeats. We improved the library construction process using a "filtration" procedure to retain only fully coding modules that were recombined to recreate sequence diversity. The final library named Lib2.1 contains 1.7×10(9) independent clones. Here, we used phage display to select, from the previously described library or from the new library, new specific αRep proteins binding to four different non-related predefined protein targets. Specific binders were selected in each case. The results show that binders with various sizes are selected including relatively long sequences, with up to 7 repeats. ITC-measured affinities vary with Kd values ranging from micromolar to nanomolar ranges. The formation of complexes is associated with a significant thermal stabilization of the bound target protein. The crystal structures of two complexes between αRep and their cognate targets were solved and show that the new interfaces are established by the variable surfaces of the repeated modules, as well by the variable N-cap residues. These results suggest that αRep library is a new and versatile source of tight and specific binding proteins with favorable biophysical properties.
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