Quantum dot-fluorescent protein pairs as novel fluorescence resonance energy transfer probes.
Fluorescence resonance energy transfer (FRET) characteristics, including the efficiency, donor-acceptor distance, and binding strength of six fluorescent protein (FP)-quantum dot (QD) pairs were quantified, demonstrating that FPs are efficient acceptors for QD donors with up to 90% quenching of QD fluorescence and that polyhistidine coordination to QD core-shell surface is a straightforward and effective means of conjugating proteins to commercially available QDs. This provides a novel approach to developing QD-based FRET probes for biomedical applications.
Dennis
Allison M
AM
Department of Biomedical Engineering, Georgia Institute of Technology and Emory University, 313 Ferst Drive, Atlanta, Georgia 30332, USA.
Bao
Gang
G
D003460:Crystallization / Q000379:methods*; D031541:Fluorescence Resonance Energy Transfer / Q000379:methods*; D006639:Histidine / Q000737:chemistry*; D008422:Materials Testing; D008968:Molecular Conformation; D015336:Molecular Probe Techniques; D036103:Nanotechnology / Q000379:methods*; D010316:Particle Size; D045663:Quantum Dots
C033223:polyhistidine; D006639:Histidine