ArticleBioscience reports2015
Specific GFP-binding artificial proteins (αRep): a new tool for in vitro to live cell applications.
Article in Bioscience reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Structural Insights into the Binding of Red Fluorescent Protein mCherry-Specific Nanobodies.International journal of molecular sciences · 2023Article
- Occupation of a thermoresistant-scaffold (αRep) at SP1-NC cleavage site disturbs the function of HIV-1 protease.Bioscience reports · 2020Article
- bioPROTACs as versatile modulators of intracellular therapeutic targets including proliferating cell nuclear antigen (PCNA).Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Ligand-induced conformational switch in an artificial bidomain protein scaffold.Scientific reports · 2019Article
- 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
- Reduced Fluorescent Protein Switching Fatigue by Binding-Induced Emissive State Stabilization.International journal of molecular sciences · 2017Article
- Performance of MDockPP in CAPRI rounds 28-29 and 31-35 including the prediction of water-mediated interactions.Proteins · 2017Article
- Destabilizing an interacting motif strengthens the association of a designed ankyrin repeat protein with tubulin.Scientific reports · 2016Article
- Article
Corrections and comments
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Authors and funding
11 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A family of artificial proteins, named αRep, based on a natural family of helical repeat was previously designed. αRep members are efficiently expressed, folded and extremely stable proteins. A large αRep library was constructed creating proteins with a randomized interaction surface. In the present study, we show that the αRep library is an efficient source of tailor-made specific proteins with direct applications in biochemistry and cell biology. From this library, we selected by phage display αRep binders with nanomolar dissociation constants against the GFP. The structures of two independent αRep binders in complex with the GFP target were solved by X-ray crystallography revealing two totally different binding modes. The affinity of the selected αReps for GFP proved sufficient for practically useful applications such as pull-down experiments. αReps are disulfide free proteins and are efficiently and functionally expressed in eukaryotic cells: GFP-specific αReps are clearly sequestrated by their cognate target protein addressed to various cell compartments. These results suggest that αRep proteins with tailor-made specificity can be selected and used in living cells to track, modulate or interfere with intracellular processes.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.