Langmuir-Blodgett Films of Streptavidin-Conjugated Phycoerythrin Bound toBiotinylated Monolayers. (Reannouncement with New Availability Information)

摘要

The Langmuir-Blodgett technique has been used to simultaneously orient and couplethe photodynamic, water soluble protein, phycoerythrin, to a biotin derivatized phospholipid monolayer film. It was found that both avidin and streptavidin phycoerythrin conjugates will preferentially adsorb to the biotinylated lipid monolayer films while at the air-water interface. Pressure-area isotherms indicate that oriented monolayer films are formed with the hydrophilic biotin binding sites exposed to the four biotin binding sites on avidin and streptavidin in the conjugated proteins. The binding of protein to the lipid films was determined by probing the characteristic, intense fluorescence of the phycoerythrin at 576 nm. The measurements were carried out on monolayer films transferred onto solid glass supports, exciting the samples with 496 nm light and scanning the emission form 515 to 670 nm. It was determined that avidin conjugated proteins complex to the biotin lipid monolayer through both specific and non-specific binding mechanisms, while the streptavidin-phycoerythrin binds by what appears to be only a specific (biotin-streptavidin) mechanism. Langmuir-Blodgett, phycoerythrin, photodynamic proteins, monolayer, biotin, streptavidin, avidin.