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Updated: May 20, 2026

Analyzing DNA-Protein Interactions with Streptavidin-Based Biolayer Interferometry
Published on: January 17, 2025
Modeling negative cooperativity in streptavidin adsorption onto biotinylated microtubules
Siheng He1, Amy T Lam, Yolaine Jeune-Smith
1Department of Biomedical Engineering, Columbia University, New York, New York 10027, United States.
Abstract:
The nanoscale architecture of binding sites can result in complex binding kinetics. Here, the adsorption of streptavidin and neutravidin to biotinylated microtubules is found to exhibit negative cooperativity due to electrostatic interactions and steric hindrance. This behavior is modeled by a newly developed kinetic analogue of the Fowler-Guggenheim adsorption model. The complex adsorption kinetics of streptavidin to biotinylated structures needs to be considered when these intermolecular bonds are employed in self-assembly and nanobiotechnology.

