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

ABSTRACT: 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 biotiny

SUBMITTER: Sedlak SM 

PROVIDER: S-EPMC5716544 | biostudies-literature | 2017

REPOSITORIES: biostudies-literature