ArticlePloS one2012
Development of a tetrameric streptavidin mutein with reversible biotin binding capability: engineering a mobile loop as an exit door for biotin.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 26 citations in OpenAlex.
- An engineered redox-switchable streptavidin mutein enables the high-affinity capture and efficient elution of biotinylated ligands.Protein science : a publication of the Protein Society · 2025Article
- Production of mutant streptavidin protein and investigation of its effect on the performance of streptavidin.Iranian journal of basic medical sciences · 2023Article
- A novel multimeric sCD19-streptavidin fusion protein for functional detection and selective expansion of CD19-targeted CAR-T cells.Cancer medicine · 2022Article
- Thiol-Cleavable Biotin for Chemical and Enzymatic Biotinylation and Its Application to Mitochondrial TurboID Proteomics.Journal of the American Society for Mass Spectrometry · 2021Article
- Engineering a disulfide-gated switch in streptavidin enables reversible binding without sacrificing binding affinity.Scientific reports · 2020Article
- Immobilization of Growth Factors for Cell Therapy Manufacturing.Frontiers in bioengineering and biotechnology · 2020Review
- Chemical Derivatization of Affinity Matrices Provides Protection from Tryptic Proteolysis.Journal of proteome research · 2019Article
- Site-specific anchoring aptamer C2NP on DNA origami nanostructures for cancer treatment.RSC advances · 2018Article
- Identification of a Flavonoid Glucosyltransferase Involved in 7-OH Site Glycosylation in Tea plants (Camellia sinensis).Scientific reports · 2017Article
- A simple approach for preparation of affinity matrices: Simultaneous purification and reversible immobilization of a streptavidin mutein to agarose matrix.Scientific reports · 2017Article
- Functional loop dynamics of the streptavidin-biotin complex.Scientific reports · 2015Article
- The structure of the SBP-Tag-streptavidin complex reveals a novel helical scaffold bridging binding pockets on separate subunits.Acta crystallographica. Section D, Biological crystallography · 2013Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A novel form of tetrameric streptavidin has been engineered to have reversible biotin binding capability. In wild-type streptavidin, loop(3-4) functions as a lid for the entry and exit of biotin. When biotin is bound, interactions between biotin and key residues in loop(3-4) keep this lid in the closed state. In the engineered mutein, a second biotin exit door is created by changing the amino acid sequence of loop(7-8). This door is mobile even in the presence of the bound biotin and can facilitate the release of biotin from the mutein. Since loop(7-8) is involved in subunit interactions, alteration of this loop in the engineered mutein results in an 11° rotation between the two dimers in reference to wild-type streptavidin. The tetrameric state of the engineered mutein is stabilized by a H127C mutation, which leads to the formation of inter-subunit disulfide bonds. The biotin binding kinetic parameters (k(off) of 4.28×10(-4) s(-1) and K(d) of 1.9×10(-8) M) make this engineered mutein a superb affinity agent for the purification of biotinylated biomolecules. Affinity matrices can be regenerated using gentle procedures, and regenerated matrices can be reused at least ten times without any observable reduction in binding capacity. With the combination of both the engineered mutein and wild-type streptavidin, biotinylated biomolecules can easily be affinity purified to high purity and immobilized to desirable platforms without any leakage concerns. Other potential biotechnological applications, such as development of an automated high-throughput protein purification system, are feasible.
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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.