6533b7d0fe1ef96bd125b9be
RESEARCH PRODUCT
Interaction between biotin lipids and streptavidin in monolayers: formation of oriented two-dimensional protein domains induced by surface recognition.
Rainer BlankenburgP. MellerChristian SalesseHelmut Ringsdorfsubject
StreptavidinChemical PhenomenaSurface PropertiesProtein domainBiotinBiochemistrychemistry.chemical_compoundBiotinBacterial ProteinsMonolayerFluorescence microscopebiologyChemistryChemistry PhysicalPhosphatidylethanolaminestechnology industry and agricultureMembranes ArtificialHydrogen-Ion ConcentrationAvidinFluorescenceLipidsSpectrometry FluorescenceSolubilityBiotinylationbiology.proteinBiophysicsSpectrophotometry UltravioletStreptavidinAvidindescription
Highly specific ligand-receptor interactions generally characterize surface recognition reactions. Such processes can be simulated by streptavidin-biotin-specific binding. Biotin lipids have thus been synthesized, and their interaction with streptavidin (or avidin) at the air-water interface was directly shown by measurement of surface pressure isotherms and fluorescence microscopy. These proteins interact with the biotin lipid monolayer via specific binding or nonspecific adsorption. Both phenomena were clearly distinguished by use of the inactivated form of streptavidin. The binding of fluorescein-labeled streptavidin to monolayers was also directly observed by fluorescence microscopy. The fluorescence of the protein domains is directly related to the state of polarization of the exciting light. This anisotropy can only be explained by the formation of oriented two-dimensional biotin lipid-streptavidin domains.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1989-10-01 | Biochemistry |