Direct force measurements of the streptavidin-biotin interaction.
The interaction between streptavidin and its ligand, biotin, were studied by direct force measurements. The complimentary approaches of surface force apparatus (SFA) and atomic force microscopy (AFM) were used to elucidate both long-range and short-range adhesive interactions of the streptavidin biotin interaction. The high spatial resolution of the SFA provided a detailed profile of the intersurface forces of apposing surfaces functionalized with streptavidin and biotin. Measurements obtained by the SFA corresponded to long and intermediate-range forces that are important in determining ligand receptor association. AFM was used to measure the unbinding force of individual streptavidin biotin complexes. These measurements revealed the short-range interactions (i.e. hydrophobic and hydrogen bonding forces) that stabilize the intermolecular bond.
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Related Subject Headings
- Thermodynamics
- Surface Properties
- Streptavidin
- Protein Engineering
- Protein Binding
- Microscopy, Atomic Force
- Ligands
- Hydrogen Bonding
- Biotin
- Biotechnology
Citation
Published In
DOI
ISSN
Publication Date
Volume
Issue
Start / End Page
Related Subject Headings
- Thermodynamics
- Surface Properties
- Streptavidin
- Protein Engineering
- Protein Binding
- Microscopy, Atomic Force
- Ligands
- Hydrogen Bonding
- Biotin
- Biotechnology