6533b7cefe1ef96bd12579a1
RESEARCH PRODUCT
Specific recognition and formation of two- dimensional streptavidin domains in monolayers: applications to molecular devices
Christian SalesseRainer BlankenburgMichael AhlersDavid W. GraingerHelmut RingsdorfP. Mellersubject
StreptavidinBiotin bindingProtein domaintechnology industry and agricultureMetals and AlloysSurfaces and InterfacesSurfaces Coatings and FilmsElectronic Optical and Magnetic Materialschemistry.chemical_compoundCrystallographyBiotinchemistryBiotinylationMonolayerMaterials ChemistryFluorescence microscopeProtein crystallizationdescription
Abstract By virtue of the high-affinity specific interaction between the vitamin, biotin, and the protein, streptavidin, monolayers of synthetic lipids with biotin headgroups can tightly bind streptavidin at the lipid-water interface. Through this specific recognition fluorescently-labelled streptavidin spontaneously organizes in the plane of the interface to form large protein domains, directly visible in situ by fluorescence microscopy and exhibiting optical anisotropy. Further structural characterization has shown that these domains are two-dimensional protein crystals. Correlation with the known three-dimensional crystal structure of streptavidin indicates that two of streptavidin's four biotin binding sites are free for further derivatization to create multilayered organized protein molecular devices.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1989-11-01 | Thin Solid Films |