title: Modeling negative cooperativity in streptavidin adsorption onto biotinylated microtubules.
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.
authors: Department of Biomedical Engineering, Columbia University, New York, New York 10027, United States.
authors: Siheng
authors: S
authors: He
authors: Amy T
authors: AT
authors: Lam
authors: Yolaine
authors: Y
authors: Jeune-Smith
authors: Henry
authors: H
authors: Hess
mesh_terms: D000327:Adsorption; D001360:Avidin / Q000737:chemistry; D001710:Biotin / Q000737:chemistry*; D019921:Biotinylation; D007700:Kinetics; D008870:Microtubules / Q000737:chemistry*; D008958:Models, Molecular; D019809:Streptavidin / Q000737:chemistry*; D013499:Surface Properties
chemical_list: C093483:neutravidin; D001360:Avidin; D001710:Biotin; D019809:Streptavidin