ArticleNature nanotechnology2016
Monovalent Strep-Tactin for strong and site-specific tethering in nanospectroscopy.
Article in Nature nanotechnology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Revealing the Control Mechanisms of pH on the Solution Properties of Chitin via Single-Molecule Studies.Molecules (Basel, Switzerland) · 2023Article
- Directed evolution of orthogonal RNA-RBP pairs through library-vs-library in vitro selection.Nucleic acids research · 2022Article
- Streptavidin/biotin: Tethering geometry defines unbinding mechanics.Science advances · 2020Article
- Next Generation Methods for Single-Molecule Force Spectroscopy on Polyproteins and Receptor-Ligand Complexes.Frontiers in molecular biosciences · 2020Review
- Structural and mechanistic insights into mechanoactivation of focal adhesion kinase.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Functional expression of monomeric streptavidin and fusion proteins in Escherichia coli: applications in flow cytometry and ELISA.Applied microbiology and biotechnology · 2018Article
- Rapid Characterization of a Mechanically Labile α-Helical Protein Enabled by Efficient Site-Specific Bioconjugation.Journal of the American Chemical Society · 2017Article
- Article
- Post-Translational Sortase-Mediated Attachment of High-Strength Force Spectroscopy Handles.ACS omega · 2017Article
- Synthetic mimics of biotin/(strept)avidin.Chemical Society reviews · 2017Review
- The principles and applications of avidin-based nanoparticles in drug delivery and diagnosis.Journal of controlled release : official journal of the Controlled Release Society · 2017Review
- Monodisperse measurement of the biotin-streptavidin interaction strength in a well-defined pulling geometry.PloS one · 2017Article
- pH-Dependent Interactions in Dimers Govern the Mechanics and Structure of von Willebrand Factor.Biophysical journal · 2016Article
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Strep-Tactin, an engineered form of streptavidin, binds avidly to the genetically encoded peptide Strep-tag II in a manner comparable to streptavidin binding to biotin. These interactions have been used in protein purification and detection applications. However, in single-molecule studies, for example using atomic force microscopy-based single-molecule force spectroscopy (AFM-SMFS), the tetravalency of these systems impedes the measurement of monodispersed data. Here, we introduce a monovalent form of Strep-Tactin that harbours a unique binding site for Strep-tag II and a single cysteine that allows Strep-Tactin to specifically attach to the atomic force microscope cantilever and form a consistent pulling geometry to obtain homogeneous rupture data. Using AFM-SMFS, the mechanical properties of the interaction between Strep-tag II and monovalent Strep-Tactin were characterized. Rupture forces comparable to biotin:streptavidin unbinding were observed. Using titin kinase and green fluorescent protein, we show that monovalent Strep-Tactin is generally applicable to protein unfolding experiments. We expect monovalent Strep-Tactin to be a reliable anchoring tool for a range of single-molecule studies.
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Registered trials
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