Monodisperse measurement of the biotin-streptavidin interaction strength in a well-defined pulling geometry

The widely used interaction of the homotetramer streptavidin with the small molecule biotin has been intensively studied by force spectroscopy and has become a model system for receptor ligand interaction. However, streptavidin's tetravalency results in diverse force propagation pathways throug...

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Veröffentlicht in:PloS one 2017-12, Vol.12 (12), p.e0188722-e0188722
Hauptverfasser: Sedlak, Steffen M, Bauer, Magnus S, Kluger, Carleen, Schendel, Leonard C, Milles, Lukas F, Pippig, Diana A, Gaub, Hermann E
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creator Sedlak, Steffen M
Bauer, Magnus S
Kluger, Carleen
Schendel, Leonard C
Milles, Lukas F
Pippig, Diana A
Gaub, Hermann E
description The widely used interaction of the homotetramer streptavidin with the small molecule biotin has been intensively studied by force spectroscopy and has become a model system for receptor ligand interaction. However, streptavidin's tetravalency results in diverse force propagation pathways through the different binding interfaces. This multiplicity gives rise to polydisperse force spectroscopy data. Here, we present an engineered monovalent streptavidin tetramer with a single cysteine in its functional subunit that allows for site-specific immobilization of the molecule, orthogonal to biotin binding. Functionality of streptavidin and its binding properties for biotin remain unaffected. We thus created a stable and reliable molecular anchor with a unique high-affinity binding site for biotinylated molecules or nanoparticles, which we expect to be useful for many single-molecule applications. To characterize the mechanical properties of the bond between biotin and our monovalent streptavidin, we performed force spectroscopy experiments using an atomic force microscope. We were able to conduct measurements at the single-molecule level with 1:1-stoichiometry and a well-defined geometry, in which force exclusively propagates through a single subunit of the streptavidin tetramer. For different force loading rates, we obtained narrow force distributions of the bond rupture forces ranging from 200 pN at 1,500 pN/s to 230 pN at 110,000 pN/s. The data are in very good agreement with the standard Bell-Evans model with a single potential barrier at Δx0 = 0.38 nm and a zero-force off-rate koff,0 in the 10-6 s-1 range.
doi_str_mv 10.1371/journal.pone.0188722
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subjects Atomic beam spectroscopy
Atomic force microscopy
Binding sites
Biology and Life Sciences
Biotin
Cysteine
Dosage and administration
Experiments
Health aspects
Immobilization
Interfaces
Ligands
Measurement
Mechanical properties
Medicine and Health Sciences
Microscopy
Nanoparticles
Physical Sciences
Polyethylene glycol
Potential barriers
Research and Analysis Methods
Spectroscopy
Spectrum analysis
Stoichiometry
Streptavidin
title Monodisperse measurement of the biotin-streptavidin interaction strength in a well-defined pulling geometry
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