Abstract
The specific binding of proteins to functionalized monolayers on aqueous subphases has been characterized by neutron reflectivity measurements. As a model for the investigation of a recognition process on a molecular length scale, streptavidin (SA) and biotin were chosen because of the high specific affinity between them. Reflectivities from the aqueous (NaCl/H2O or NaCl/D2O) surfaces covered with the biotin-lipid monolayers before and after the adsorption of proteins were collected with a novel, fixed wavelength liquid surface neutron reflectometer. In quantitative terms, binding was found to occur at a biotin surface concentration as low as 1 molecule/1250 Å2 (compare to ∼ 1 molecule/40 Å2 for a densely packed monolayer). The reflectivity data are consistent with the formation of a monomolecular layer of protein at the interface, directly underneath the lipid monolayer. The thickness of the protein film is 44 ± 2 Å, comparable in size to the the smallest axis of the unit cell of 3-dimensional SA crystals (48 Å).KeywordsLipid MonolayerProtein FilmMonomolecular LayerScatter Length DensityNeutron ReflectivityThese keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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