Quantum Dot−Fluorescent Protein Pairs as Novel Fluorescence Resonance Energy Transfer Probes
Allison M. Dennis, Gang Bao
Abstract
Allison M. Dennis, Gang Bao
Abstract
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.
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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.
Key concepts: Förster resonance energy transfer, Quantum dot, Fluorescence, Fluorescence in the life sciences, Quenching (fluorescence), Acceptor, Energy transfer, Chemistry