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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Bibliographic Details
Published in:Langmuir 2004-08, Vol.20 (18), p.7720-7728
Main Authors: Sapsford, Kim E, Medintz, Igor L, Golden, Joel P, Deschamps, Jeffery R, Uyeda, Harry Tetsuo, Mattoussi, Hedi
Format: Article
Language:English
Subjects:
Avidin - chemistry
Biosensing Techniques - instrumentation
Biosensing Techniques - methods
Biotinylation
Carrier Proteins - chemistry
Fluorescence Resonance Energy Transfer - instrumentation
Fluorescence Resonance Energy Transfer - methods
Maltose-Binding Proteins
Membrane Proteins - chemistry
Nanotechnology
Quantum Dots
Sensitivity and Specificity
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Summary: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.
ISSN:0743-7463
1520-5827
DOI:10.1021/la049263n