ArticlePloS one2013
A polypeptide-DNA hybrid with selective linking capability applied to single molecule nano-mechanical measurements using optical tweezers.
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 8 papers.
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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.
- Optical tweezers in biomedical research - progress and techniques.Journal of medicine and life · 2024Review
- Directed evolution of orthogonal RNA-RBP pairs through library-vs-library in vitro selection.Nucleic acids research · 2022Article
- Simultaneous sensing and imaging of individual biomolecular complexes enabled by modular DNA-protein coupling.Communications chemistry · 2020Article
- The Anti-Aggregation Holdase Hsp33 Promotes the Formation of Folded Protein Structures.Biophysical journal · 2020Article
- Single-molecule mechanics of protein-labelled DNA handles.Beilstein journal of nanotechnology · 2016Article
- Monovalent Strep-Tactin for strong and site-specific tethering in nanospectroscopy.Nature nanotechnology · 2016Article
- Acoustic force spectroscopy.Nature methods · 2015Article
- Designing disorder: Tales of the unexpected tails.Intrinsically disordered proteinsReview
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Many applications in biosensing, biomaterial engineering and single molecule biophysics require multiple non-covalent linkages between DNA, protein molecules, and surfaces that are specific yet strong. Here, we present a novel method to join proteins and dsDNA molecule at their ends, in an efficient, rapid and specific manner, based on the recently developed linkage between the protein StrepTactin (STN) and the peptide StrepTag II (ST). We introduce a two-step approach, in which we first construct a hybrid between DNA and a tandem of two STs peptides (tST). In a second step, this hybrid is linked to polystyrene bead surfaces and Maltose Binding Protein (MBP) using STN. Furthermore, we show the STN-tST linkage is more stable against forces applied by optical tweezers than the commonly used biotin-Streptavidin (STV) linkage. It can be used in conjunction with Neutravidin (NTV)-biotin linkages to form DNA tethers that can sustain applied forces above 65 pN for tens of minutes in a quarter of the cases. The method is general and can be applied to construct other surface-DNA and protein-DNA hybrids. The reversibility, high mechanical stability and specificity provided by this linking procedure make it highly suitable for single molecule mechanical studies, as well as biosensing and lab on chip applications.
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Registered trials
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