F?rster resonance energy transfer (FRET) from luminescent terbium complexes (LTC) as donors to semiconductor quantum dots (QDs) as acceptors allows extraordinary large FRET efficiencies due to the long F?rster distances afforded. Moreover, time-gated detection permits an efficient suppression of autofluorescent background leading to sub-picomolar detection limits even within multiplexed detection formats. These characteristics make FRET-systems with LTC and QDs excellent candidates for clinical diagnostics. So far, such proofs of principle for highly sensitive multiplexed biosensing have only been performed under optimized buffer conditions and interactions between real-life clinical media such as human serum or plasma and LTC-QD-FRET-systems have not yet been taken into account. Here we present an extensive spectroscopic analysis of absorption, excitation and emission spectra along with the luminescence decay times of both the single components as well as the assembled FRET-systems in TRIS-buffer, TRIS-buffer with 2% bovine serum albumin, and fresh human plasma. Moreover, we evaluated homogeneous LTC-QD FRET assays in QD conjugates assembled with either the well-known, specific biotin-streptavidin biological interaction or, alternatively, the metal-affinity coordination of histidine to zinc. In the case of conjugates assembled with biotin-streptavidin no significant interference with the optical and binding properties occurs whereas the histidine-zinc system appears to be affected by human plasma.
Medintz, IL; Matoussi, H. Quantum dot-based resonance energy transfer and its growing application in biology. Phys. Chem. Chem. Phys 2009, 11, 17–45.
[3]
Sekar, RB; Periasamy, A. Fluorescence Resonance Energy Transfer (FRET) microscopy imaging of live cell protein localization. J. Cell. Biol 2003, 5, 629–633.
[4]
Miller, JN. Fluorescence energy transfer methods in bioanalysis. Analyst 2005, 130, 265–270.
[5]
Giestas, L; Ferreira, GNM; Baptista, PV; Lima, JC. Multiplexed spectral coding for simultaneous detection of DNA hybridization reactions based on FRET. Sens. Actuat. B 2008, 134, 146–157.
[6]
Wu, P; Brand, L. Resonance energy transfer: Methods and applications. Anal. Biochem 1994, 218, 1–13.
[7]
Mitra, RD; Silva, CM; Youvan, DC. Fluorescence resonance energy transfer between blue-emitting and red-shifted excitation derivatives of the green xuorescent protein. Gene 1996, 173, 13–17.
[8]
Resch-Genger, U; Grabolle, M; Cavaliere-Jaricot, S; Nitschke, R; Nann, T. Quantum dots versus dyes as fluorescent labels. Nat. Methods 2008, 5, 763–775.
[9]
Chudakov, DM; Matz, MV; Lukyanov, S; Lukyanov, KA. Fluorescent proteins and their applications in imaging living cells and tissues. Physiol. Rev 2010, 90, 1103–1163.
[10]
Woehler, A; Wlodarczyk, J; Neher, E. Signal/noise analysis of FRET-based sensors. Biophys. J 2010, 99, 2344–2354.
[11]
Selvin, PR. Lanthanide-based resonance energy transfer. IEEE J. Sel. Top. Quant. Electron 1996, 2, 1077–1087.
[12]
Van der Meer, BW; Coker, G; Chen, SYS. Resonance Energy Transfer: Theory and Data; VCH: New York, NY, and Cambridge, MA, USA, 1994.
[13]
Charbonnière, L; Hildebrandt, N; Ziessel, RF; L?hmannsr?ben, HG. Lanthanides to quantum dots resonance energy transfer in time-resolved fluoro-immunoassays and luminescence microscopy. J. Am. Chem. Soc 2006, 128, 12800–12809.
[14]
H?rm?, H; Souka, T; Shavel, A; Gaponik, N; Weller, H. Luminescent energy transfer between cadmium telluride nanoparticle and lanthanide(III) chelate in competitive bioaffinity assays of biotin and estradiol. Anal. Chim. Acta 2007, 604, 177–183.
[15]
Soini, E; L?vgren, T; Reimer, CB. Time-resolved fluorescence of lanthanide probes and applications in biotechnology. CRC Crit. Rev. Anal. Chem 1987, 18, 105–154.
[16]
Gei?ler, D; Charbonnière, L; Ziessel, R; Butlin, N; L?hmannsr?ben, H-G; Hildebrandt, N. Quantum-dot biosensors for ultrasensitive multiplexed diagnostics. Angew. Chem. Int. Ed 2010, 49, 1396–1401.
[17]
Josephson, B; Dahlberg, J. Variations in the cell content and chemical composition of the human blood due to age, sex and season. Scand. J. Clin. Lab. Invest 1952, 4, 216–236.
[18]
Abugo, OO; Nair, R; Lakowicz, JR. Fluorescence properties of rhodamine 800 in whole blood and plasma. Anal. Biochem 2000, 279, 142–150.
[19]
Sapsford, KE; Farrell, D; Steven Sun, S; Rasooly, A; Mattoussi, H; Medintz, IL. Monitoring of enzymatic proteolysis on a electroluminescent-CCD microchip platform using quantum dot-peptide substrates. Sens. Actuat. B 2009, 139, 13–21.
[20]
Dennis, AM; Sotto, D; Mei, BC; Medintz, IL; Mattoussi, H; Bao, G. Surface ligand effects on metal-affinity coordination to quantum dots: Implications for nanoprobe self-assembly. Bioconjug. Chem 2010, 21, 1160–1170.
[21]
Susumu, K; Oh, E; Delehanty, JB; Blanco-Canosa, JB; Johnson, B; Jain, V; Hervey, WJ; Algar, WR; Boeneman, K; Dawson, P; et al. Multifunctional compact zwitterionic ligands for preparing robust biocompatible semiconductor quantum dots and gold nanoparticles. J Am Chem Soc 2011, 133, 9480–9496. and references 32–36 therein.
[22]
Morgner, F; Gei?ler, D; Stufler, S; Butlin, NG; L?hmannsr?ben, HG; Hildebrandt, N. A quantum-dot based molecular ruler for multiplexed optical analysis. Angew. Chem. Int. Ed 2010, 49, 7570–7574.
[23]
Siepak, J. Terbium chelate labels for fluorescence immunoassays. Analyst 1989, 114, 529–531.
[24]
Wang, Y; Feng, L; Jiang, C. Fluorimetric study of the interaction between human serum albumin and quinolones-terbium complex and its application. Spectrochim. Acta A 2005, 61, 2909–2914.
[25]
Moreno, F; Cortijo, M; González-Jiménez, J. The fluorescent probe prodan characterizes the warfarin binding site on human serum albumin. Photochem. Photobiol 1999, 69, 8–15.
[26]
Barik, A; Mishra, B; Kunwar, A; Priyadarsini, KI. Interaction of curcumin with human serum albumin: Thermodynamic properties, fluorescence energy transfer and denaturation effects. Chem. Phys. Lett 2007, 436, 239–243.
[27]
Xiao, Q; Huang, S; Qi, ZD; Zhou, B; He, ZK; Liu, Y. Conformation, thermodynamics and stoichiometry of HSA adsorbed to colloidal CdSe/ZnS quantum dots. Biochim. Biophys. Acta 2008, 1784, 1010–1027.
[28]
Vannoy, CH; Leblanc, RM. Effects of DHLA-capped CdSe/ZnS quantum dots on the fibrillation of human serum albumin. J. Phys. Chem 2010, 114, 10881–10888.
Jiang, J; Oberd?rster, G; Biswas, P. Characterization of size, surface charge, and agglomeration state of nanoparticle dispersions for toxicological studies. J. Nanopart. Res 2009, 11, 77–89.
[31]
Hardman, R. A toxicologic review of quantum dots: Toxicity depends on physicochemical and environmental factors. Environ. Health Perspect 2006, 114, 165–172.
[32]
Wild, D. The Immunoassay Handbook, 3rd ed ed.; Elsevier Science: Amsterdam, The Netherlands, 2005.
[33]
Diamandis, E. Immunoassays with time-resolved fluorescence spectroscopy: Principles and applications. Clin. Biochem 1988, 21, 139–150.
[34]
Weber, PC; Ohlendorf, DH; Wendoloski, JJ; Salemme, FR. Structural origins of high-affinity biotin binding to streptavidin. Science 1989, 243, 85–88.
[35]
Warnera, MG; Gratea, JW; Tyler, A; Ozanicha, RM; Millera, KD; Loub, J; Marks, JD; Bruckner-Lea, CJ. Quantum dot immunoassays in renewable surface column and 96-well plate formats for the fluorescence detection of botulinum neurotoxin using high-affinity antibodies. Biosens. Bioelectron 2009, 25, 179–184.
[36]
Sch?nheyder, H; Andersen, P. Effects of bovine serum albumin on antibody determination by the enzyme-linked immunosorbent assay. J. Immunol. Meth 1984, 72, 251–259.
[37]
Mendel, CM; Mendel, DB. Non-specific binding. The problem, and a solution. Biochem. J 1985, 228, 269–272.
[38]
Prasuhn, DE; Blanco-Canosa, JB; Vora, GJ; Delehanty, JB; Susumu, K; Mei, BC; Dawson, PE; Medintz, IL. Combining chemoselective ligation with polyhistidine-driven self-assembly for the modular display of biomolecules on quantum dots. ACS Nano 2010, 4, 267–278.
[39]
Sapsford, KE; Pons, T; Medintz, IL; Higashiya, S; Brunel, FM; Dawson, PE; Mattoussi, H. Kinetics of metal-affinity driven self-assembly between proteins or peptides and CdSe-ZnS quantum dots. J. Phys. Chem. C 2007, 111, 11528–11538.
[40]
Medintz, IL; Stewart, MH; Trammell, SA; Susumu, K; Delehanty, JB; Mei, BC; Melinger, JS; Blanco-Canosa, JB; Dawson, PE; Mattoussi, H. Quantum dot dopamine bioconjugates function as redox coupled assemblies for in vitro and intracellular pH sensing. Nat. Mater 2010, 9, 676–684.
[41]
Prasuhn, DE; Deschamps, JR; Susumu, K; Stewart, MH; Boeneman, K; Blanco-Canosa, JB; Dawson, PE; Medintz, IL. Polyvalent display and packing of peptides and proteins on semiconductor quantum dots: Predicted versus experimental results. Small 2010, 6, 555–564.
[42]
Guthans, SL; Morgan, WT. The interaction of zinc, nickel and cadmium with serum albumin and histidine-rich glycoprotein assessed by equilibrium dialysis and immunoadsorbent chromatography. Arch. Biochem. Biophys 1982, 218, 320–328.
[43]
Morgan, WT. Interaction of the histidine-rich glycoprotein of serum with metals. Biochemistry 1981, 20, 1054–1061.
[44]
Algar, WR; Prasuhn, DE; Stewart, M; Jennings, Travis; Blanco-Canosa, JB; Dawson, P; Medintz, IL. The controlled display of biomolecules on nanoparticles: A challenge suited to bioorthogonal chemistry. Bioconjug. Chem 2011, 22, 825–858.
[45]
Boeneman, K; Delehanty, JB; Stewart, MH; Susumu, K; Medintz, IL. Intracellular bioconjugation of targeted proteins with semiconductor quantum dots. J. Am. Chem. Soc 2010, 132, 5975–5977.
[46]
Delehanty, JB; Boeneman, K; Bradburne, CE; Robertson, K; Bongard, JE; Medintz, IL. Peptides for specific intracellular delivery and targeting of nanoparticles: Implications for developing nanoparticle-mediated drug delivery. Ther. Deliv 2010, 1, 411–433.