Surface-immobilized self-assembled protein-based quantum dot nanoassemblies

Luminescent semiconductor quantum dot (QD)-based optical biosensors have the potential to overcome many of the limitations associated with using conventional organic dyes for biodetection. We have previously demonstrated a hybrid QD-protein-based fluorescence resonance energy transfer (FRET) sensor....

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Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1992. - 20(2004), 18 vom: 31. Aug., Seite 7720-8
1. Verfasser: Sapsford, Kim E (VerfasserIn)
Weitere Verfasser: Medintz, Igor L, Golden, Joel P, Deschamps, Jeffery R, Uyeda, Harry Tetsuo, Mattoussi, Hedi
Format: Aufsatz
Sprache:English
Veröffentlicht: 2004
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, U.S. Gov't, Non-P.H.S. Carrier Proteins Maltose-Binding Proteins Membrane Proteins neutravidin Avidin 1405-69-2
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245 1 0 |a Surface-immobilized self-assembled protein-based quantum dot nanoassemblies 
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520 |a Luminescent semiconductor quantum dot (QD)-based optical biosensors have the potential to overcome many of the limitations associated with using conventional organic dyes for biodetection. We have previously demonstrated a hybrid QD-protein-based fluorescence resonance energy transfer (FRET) sensor. Although the QD acted as an energy donor and a protein scaffold in the sensor, recognition and specificity were derived from the proteins. Transitioning this hybrid prototype sensor into flow cells and integrated devices will require a surface-immobilization strategy that allows the QD-based sensor to sample the environment and still maintain a distinct protein-covered QD architecture. We demonstrate a self-assembled strategy designed to accomplish this. Using glass slides coated with a monolayer of neutravidin (NA) as the template, QDs with maltose binding protein (MBP) and avidin coordinated to their surface were attached to the glass slides in discrete patterns using an intermediary bridge of biotinylated MBP or antibody linkers. Control of the surface location and concentration of the QD-protein-based structures is demonstrated. The utility of this self-assembly strategy is further demonstrated by assembling a QD-protein structure that allows the QDs to engage in FRET with a dye located on the surface-covering protein 
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650 4 |a Research Support, U.S. Gov't, Non-P.H.S. 
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700 1 |a Medintz, Igor L  |e verfasserin  |4 aut 
700 1 |a Golden, Joel P  |e verfasserin  |4 aut 
700 1 |a Deschamps, Jeffery R  |e verfasserin  |4 aut 
700 1 |a Uyeda, Harry Tetsuo  |e verfasserin  |4 aut 
700 1 |a Mattoussi, Hedi  |e verfasserin  |4 aut 
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