6533b7d4fe1ef96bd1261c8d
RESEARCH PRODUCT
Molecular recognition processes at functionalized lipid surfaces: a neutron reflectivity study
M. PiepenstockJens Aage Als-nielsenMathias LöscheDavid Vakninsubject
StreptavidinChromatographyAqueous solutionChemistryMetals and AlloysAnalytical chemistrySurfaces and InterfacesSurfaces Coatings and FilmsElectronic Optical and Magnetic Materialschemistry.chemical_compoundMolecular recognitionAdsorptionMonolayerMaterials ChemistryMoleculeSurface modificationNeutrondescription
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 A2 (compare to ∼ 1 molecule/40 A2 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 A, comparable in size to the the smallest axis of the unit cell of 3-dimensional SA crystals (48 A).
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1992-04-01 | Thin Solid Films |