ArticleProtein engineering, design & selection : PEDS2016
Modular protein switches derived from antibody mimetic proteins.
Article in Protein engineering, design & selection : PEDS, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed, 23 citations in OpenAlex.
- Artificial allosteric protein switches with machine-learning-designed receptors.Nature biotechnology · 2026Article
- Autoimmune diseases: targets, biology, and drug discovery.Acta pharmacologica Sinica · 2024Review
- Chimeric Protein Switch Biosensors.Advances in biochemical engineering/biotechnology · 2024Review
- Enzyme - Switch sensors for therapeutic drug monitoring of immunotherapies.Biosensors & bioelectronics · 2023Article
- Engineering protein and DNA tools for creating DNA-dependent protein switches.Methods in enzymology · 2022Article
- FimH as a scaffold for regulated molecular recognition.Journal of biological engineering · 2021Article
- Ligand-induced conformational switch in an artificial bidomain protein scaffold.Scientific reports · 2019Article
- Quantitative and synthetic biology approaches to combat bacterial pathogens.Current opinion in biomedical engineering · 2017Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Protein switches have potential applications as biosensors and selective protein therapeutics. Protein switches built by fusion of proteins with the prerequisite input and output functions are currently developed using an ad hoc process. A modular switch platform in which existing switches could be readily adapted to respond to any ligand would be advantageous. We investigated the feasibility of a modular protein switch platform based on fusions of the enzyme TEM-1 β-lactamase (BLA) with two different antibody mimetic proteins: designed ankyrin repeat proteins (DARPins) and monobodies. We created libraries of random insertions of the gene encoding BLA into genes encoding a DARPin or a monobody designed to bind maltose-binding protein (MBP). From these libraries, we used a genetic selection system for β-lactamase activity to identify genes that conferred MBP-dependent ampicillin resistance to Escherichia coli. Some of these selected genes encoded switch proteins whose enzymatic activity increased up to 14-fold in the presence of MBP. We next introduced mutations into the antibody mimetic domain of these switches that were known to cause binding to different ligands. To different degrees, introduction of the mutations resulted in switches with the desired specificity, illustrating the potential modularity of these platforms.
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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.