CdSe-ZnS quantum dots as resonance energy transfer donors in a model protein-protein binding assay
CdSe-ZnS quantum dots as resonance energy transfer donors in a model protein-protein binding assay
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DOI：
10.1021/nl015565n
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发表时间：
2001-09-01
期刊：
影响因子：
10.8
通讯作者：
Van Orden, A
中科院分区：
文献类型：
--
作者：
Willard, DM;Carillo, LL;Van Orden, A
将生物素化牛血清白蛋白（bBSA）与四甲基罗丹明标记的链霉亲和素（SAv-TMR）偶联，通过荧光共振能量转移（FRET）从量子点供体转移到TMR受体，观察到bBSA和SAv-TMR的特异性结合.由于QD的宽吸收光谱，有效的供体激发可以在与受体的吸收光谱很好分辨的波长处发生，从而使直接受体激发最小化。供体发射光谱和受体吸收光谱的明显重叠通过将QD发射光谱尺寸调谐成与受体吸收光谱共振来实现，并且由于窄的、对称形状的CID发射光谱，供体和受体发射之间的串扰被最小化。还观察到一种额外的非特异性QD-TMR能量转移机制的证据，该机制导致QD发射猝灭而没有相应的TMR荧光增强。
Specific binding of biotinilated bovine serum albumin (bBSA) and tetramethylrhodamine-labeled streptavidin (SAv-TMR) was observed by conjugating bBSA to CdSe-ZnS core-shell quantum dots (QDs) and observing enhanced TMR fluorescence caused by fluorescence resonance energy transfer (FRET) from the QD donors to the TMR acceptors. Because of the broad absorption spectrum of the QDs, efficient donor excitation could occur at a wavelength that was well resolved from the absorption spectrum of the acceptor, thereby minimizing direct acceptor excitation. Appreciable overlap of the donor emission and acceptor absorption spectra was achieved by size-tuning the QD emission spectrum into resonance with the acceptor absorption spectrum, and cross-talk between the donor and acceptor emission was minimized because of the narrow, symmetrically shaped CID emission spectrum. Evidence for an additional, nonspecific QD-TMR energy transfer mechanism that caused quenching of the QD emission without a corresponding TMR fluorescence enhancement was also observed.