6533b85dfe1ef96bd12bf169
RESEARCH PRODUCT
Specific Protein Binding to Functionalized Interfaces
Paul K. HansmaLukas HäußlingJacob N. IsraelachviliRainer BlankenburgFranz-josef SchmittA. L. WeisenhornWolfgang KnollHelmut RingsdorfDeborah E. Leckbandsubject
Streptavidinchemistry.chemical_compoundAqueous solutionMembraneChemistryBiotinylationMonolayerSurface forces apparatusBinding siteCombinatorial chemistryPlasmondescription
We report on the characterization of specific binding reactions between streptavidin and biotinylated model membrane surfaces. Self-assembly techniques as well as the Langmuir-Blodgett-Kuhn method were employed to prepare reactive, functionalized surfaces on various solid supports in contact with the aqueous protein solution. Plasmon surface polaritons optical measurements as well as atomic force microscopy and studies with the surface forces apparatus give rather detailed information as to the streptavidin monolayer formation, the kinetics of this process (either binding site- or diffusion limited), the selectivity of the reaction at laterally heterogeneous membranes, and the involved intermolecular interaction potentials. The possibility to use these systems as universal binding matrices for other biotinylated species (e.g. antibodies) and the feasibility to carry out bioassays is shown.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1992-01-01 |