Abstract
Fluorescence resonance energy transfer (FRET) is a technique widely used to measure the distance between two points which are separated by approximately 10–80 Å. Lanthanide-based RET (LRET) is a recent modification of the technique with a number of technical advantages, yet relies on the same fundamental mechanism — subject to careful interpretation of various terms. A number of excellent reviews on FRET have been written [14, 21–28]. A recent review of LRET has also appeared [9], as well as a summary of lanthanide luminescence [29] and its application to bio-assays [30], so here we provide only a brief summary of the relevant theory.
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References
Yu, H., E.P. Diamandis. (1993) Ultrasensitive time-resolved immunofluorometric assay of prostate-specific antigen in serum and preliminary clinical studies. Clin. Chem. 39: 2108–2114.
Oser, A., W.K. Roth, G. Valet. (1988) Sensitive non-radioactive dot-blot hybridization using DNA probes labelled with chelate group substituted psoralen and quantitative detection by europium ion fluorescence. Nucleic Acids Res. 16:1181–1196.
Oser, A., M. Collasius, G. Valet. (1990) Multiple End Labeling of Oligonucleotides with Terbium Chelate-Substituted Psoralen for Time-Resolved Fluorescence Detection. Anal. Biochem. 191:295–301.
Saha, A.K., K. Kross, E.D. Kloszewski, D.A. Upson, J.L. Toner, R.A. Snow, C.D.V. Black, V.C. Desai. (1993) Time-Resolved Fluorescence of a New Europium Chelate Complex: Demonstration of Highly Sensitive Detection of Protein and DNA Samples. J. Am. Chem. Soc. 115:11032.
Hemmilä, I., S. Dakubu, V.-M. Mukkala, H. Siitari, T. Lovgren. (1984) Europium as a label in time-resolved immunofluorometric assays. Anal. Biochem. 137:335–343.
Seveus, L., M. Vaisala, I. Hemmila, H. Kojola, G.M. Roomans, E. Soini. (1994) Use of Fluorescent Europium Chelates as Labels in Microscopy Allows Glutaraldehyde Fixation and Permanent Mounting and Leads to Reduced Autofluorescence and Good Long-Term Stability. Microscopy Res. and Technique 28:149–154.
Marriott, G., M. Heidecker, E.P. Diamandis, Y. Yan-Marriott. (1994) Time-Resolved Delayed Luminescence Image Microscopy Using an Europium Ion Chelate Complex. Biophys. J. 67:957–965.
Stryer, L., D.D. Thomas, C.F. Meares. 1982. Diffusion-Enhanced Fluorescence Energy Transfer, In Ann. Rev. of Biophys. Bioeng., ed. L. J. Mullins, pp. 203–222. Palo Alto, CA: Annual Reviews, Inc.
Selvin, P.R. (1996) Lanthanide-based resonance energy transfer. IEEE J. of Selected Topics in Quantum Electronics: Lasers in Biology 2:1077–1087.
Mathis, G. (1995) Probing molecular interactions with homogeneous techniques based on rare earth cryptates and fluorescence energy transfer. Clin. Chem. 41:1391–1397.
Mathis, G. (1993) Rare Earth Cryptates and Homogeneous Fluoroimmunoassays with Human Sera. Clin. Chem. 39:1953–1959.
Selvin, P.R., T.M. Rana, J.E. Hearst. (1994) Luminescence resonance energy transfer. J. Am. Chem. Soc. 116:6029–6030.
Selvin, P.R., J.E. Hearst. (1994) Luminescence energy transfer using a terbium chelate: Improvements on fluorescence energy transfer. Proc. Natl. Acad. Sci, USA 91:10024–10028.
Selvin, P.R. 1995. Fluorescence Resonance Energy Transfer, In Methods in Enzymology, ed. K. Sauer, pp. 300–334. Orlando: Academic Press.
Heyduk, E., T. Heyduk. (1997) Thiol-reactive luminescent Europium chelates: luminescence probes for resonance energy transfer distance measurements in biomolecules. Anal. Biochem. 248:216–227.
Heyduk, E., T. Heyduk, P. Claus, J.R. Wisniewski. (1997) Conformational Changes of DNA Induced by Binding of Chironomus High Mobility Group Protein la (cHMGla). J. Biol. Chem. 272:19763–19770.
Root, D.D. (1997) In Situ molecular association of dystrophin with actin revealed by sensitized emission immuno-resonance energy transfer. Proc. Natl. Acad. Sci., USA 94.
Li, M., P.R. Selvin. (1995) Luminescent lanthanide polyaminocarboxylate chelates: the effect of chelate structure. J. Am. Chem. Soc. 117:8132–8138.
Getz, E.B., R. Cooke, P.R. Selvin. (in press) Luminescence Resonance Energy Transfer Measurements on Myosin. Biophys. J.
Xiao, M., H. Li, E.B. Getz, R. Cooke, R.G. Yount, P.R. Selvin. 1998. Luminescence Resonance Energy Transfer Measurements from the Active Site of Myosin. Presented at the Biophysical Society, Kansas City, MO 1998.
Stryer, L. (1978) Fluorescence Energy Transfer as a Spectroscopic Ruler. Ann. Rev. Biochem. 47:819–846.
Fairclough, R., H., C. Cantor, R. 1978. The use of Singlet - Singlet Energy Transfer to Study Macromolecular Assemblies, In Methods in Enzymology, ed., pp. 347–379.
Cantor, C.R., P.R. Schimmel. 1980. Biophysical Chemistry. San Francisco: W. H. Freeman and Co.
Herman, B. (1989) Resonance Energy Transfer Microscopy. Meth. Cell Bio. 30:219–243.
Coker, G., III, S.Y. Chen, B.W. van der Meer. 1994. Resonance Energy Transfer: VCH Publishers, Inc.
Clegg, R.M. (1995) Fluorescence Resonance Energy Transfer. Curr. Op. Biotech. 6: 103–110.
Clegg, R.M. 1996. Fluorescence Resonance Energy Transfer, In Fluorescence Imaging Spectroscopy and Microscopy, ed. X. F. Wang, B. Herman, pp. 179–251: John Wiley & Sons, Inc.
dos Remedios, C.G., P.D.J. Moens. 1998. Fluorescence resonance energy transfer - applications in protein chemistry, In Resonance Energy Transfer, ed. D. L. Andrews, A. A. Demidov. Chichester: John Wiley and Sons.
Bunzli, J.-C.G. 1989. Luminescent Probes, In Lanthanide Probes in Life, Chemical and Earth Sciences, Theory and Practice, ed. J.-C. G. Bunzli, G. R. Choppin, pp. 219–293. New York: Elsevier.
Sammes, P.G., G. Yahioglu. (1996) Modern Bioassays using Metal Chelates as Luminescent Probes. Modern Bioassays using Metal Chelates as Luminescent Probes 13:1–28.
Bastiaens, P.I.H., T.M. Jovin. 1998. Fluorescence Resonance Energy Transfer (FRET) Microscopy, In Cell Biology: A Laboratory Handbook, ed. J. E. Celis, pp. 136–146. New York: Academic Press.
Drexhage, K.H. (1970) Monomolecular Layers and Light. Sci. Amer. 222:108–119.
Dexter, D.L. (1953) A Theory of Sensitized Luminescence in Solids. J. Chem. Phys. 21: 836–850.
Horrocks, W.D., Jr., D.R. Sudnick. (1979) Lanthanide Ion Probes of Structure in Biology. Laser-Induced Luminescence Decay Constants Provide a Direct Measure of the Number of Metal-Coordinated Water Molecules. J. Am. Chem. Soc. 101:334–350.
Li, M., P.R. Selvin. (1997) Amine-reactive forms of a luminescent DTPA chelate of terbium and europium: Attachment to DNA and Energy Transfer Measurements. Bioconjugate Chem. 8:127–132.
Takalo, H., V.-M. Mukkala, H. Mikola, P. Liitti, I. Hemmila. (1994) Synthesis of Europium(III) Chelates Suitable for Labeling of Bioactive Molecules. Bioconjugate Chem. 5:278–282.
Selvin, P.R., J. Chen. (1998) Thiol-reactive luminescent lanthanide chelates, manuscript in preparation.
Li, H., J. Grammer, R. Cooke, P.R. Selvin, R.G. Yount. (1998) Synthesis and Spectral Characterization of a Photoaffinity ATP Analog Containing a Luminescent Lanthanide Chelate, manuscript in preparation.
>Vereb, G., E. Jares-Erijman, P.R. Selvin, T.M. Jovin. (submitted) Time and spectrally re-solved imaging microscopy of lanthanide chelates. Biophys. J.
Stryer, L. 1995. Biochemistry. San Francisco: W.H. Freeman.
Baker, J.E., I. Brust-Mascher, S. Ramachandran, L.E.W. LaConte, D.D. Thomas, (in press) A Large and Distinct Rotation Of The Myosin Light Chain Domain Upon Muscle Contraction. Proc. Nat. Acad. Sci. USA.
Irving, M., T.S. Allen, C. Sabido-David, J.S. Craik, B. Brandmeier, J. Kendrickjones, J.E.T. Corrie, D.R. Trentham, Y.E. Goldman. (1995) Tilting of the light-chain region of myosin during step length changes and active force generation in skeletal muscle. Nature 375: 688–691.
Smyzynski, C., A. A. Kasprzak. (1997) Effect of nucleotides and actin on the orientation of the light chain-bindig domain in myosin subfragment 1. Biochemistry 36:13201–13207.
Rayment, I., W.R. Rypniewski, K. Schmidt-Base, R. Smith, D.R. Tomchick, M.M. Benning, D.A. Winkelmann, G. Wesenberg, H.M. Holden. (1993 A) Three-dimensional structure of myosin subfragment-1: A molecular motor. Science 261:50–57.
Ju, J., C. Ruan, C.W. Fuller, A.N. Glazer, R.A. Mathies. (1995) Fluorescence energy transfer dye-labeled primers for DNA sequencing and analysis. Proc. Nat. Acad. Sci. USA 92: 4347–51.
Ju, J., A.N. Glazer, R.A. Mathies. (1996) Energy transfer primers: A new fluorescence labelling paradigm for DNA sequencing and analysis. Nature Medicine 2:246–249.
Bergerheim, U.S., K. Kunimi, V.P. Collins, P. Ekman. (1991) Deletion mapping of chromosomes 8, 10, and 16 in human prostatic carcinoma. Genes Chromosomes Cancer 3:215–20.
Cher, M.L., Ito, T., Weidner, N., Carroll, P.R., Jensen, R.H. (1995) Mapping of regions of physical delection on chromosome 16q in prostate cancer cells by fluorescence in situ hybridization (FISH). J. Urology 153:249–254.
Glazer, A.N., L. Stryer. (1983) Fluorescent Tandem Phycobiliprotein Conjugates: Emission Wavelength Shifting by Energy Transfer. Biophys. J. 43:383–386.
Rye, H., D. Yue S; Wemmer, M. Quesada, R. Haugland, R. Mathies,, A. Glazer. (1992) Stable fluorescent complexes of double-stranded DNA with bis-intercalating asymmetric cyanine dyes: properties and applications. Nucleic Acids Res 20:2803–2812.
Benson, S.C., R.A. Mathies, A.N. Glazer. (1993) Heterodimeric DNA-binding dyes designed for energy transfer: stability and applications of the DNA complexes. Nucl. Acids Res. 21:5720–5726.
Benson, S.C., R Singh, A.N. Glazer. (1993) Heterodimeric DNA-binding dyes designed for energy transfer: synthesis and spectroscopic properties. Nucl. Acids Res. 21:5727–5735.
Glazer, A.N., H.S. Rye. (1992) Stable Dye-DNA Intercalation Complexes as Reagents for High-Sensitivity Fluorescence Detection. Nature 359:859–861.
Glazer, A., R. Mathies. (1997) Energy-transfer fluorescent reagents for DNA analyses. Curr Opin Biotechnol 8:94–102.
Yamada, S., F. Miyoshi, K. Kano, T. Ogawa. (1981) Highly Sensitive Laser Fluorimetry of Europium(III) with l, l, l-Trifluoro-4-(2-Thienyl)-2,4-Butanedione. Anal. Chim. Acta 127: 195–198.
Weissman, S.I. (1942) Intramolecular energy transfer: the fluorescence of complexes of europium. J. Chem. Phys. 10:214.
Crosby, G.A., R.E. Whan, R.M. Alire. (1961) Intramolecular energy transfer in rare earth chelates: the role of the triplet state. J. Chem. Phys. 34:743.
Abusaleh, A., C. Meares. (1984) Excitation and De-Excitation Processes in Lanthanide Chelates Bearing Aromatic Sidechains. Photochem. & Photobiol. 39:763–769.
Kirk, W.R., W.S. Wessels, F.G. Prendergast. (1993) Lanthanide-Dependent Perturbations of Luminescence in Indolylethylenediaminetetraacetic Acid-Lanthanide Chelate. J. Phys. Chem. 97:10326–10340.
Lakowicz, J.R. 1997. Long Lifetime Metal-Ligand Complexes as Probes in Biophysics and Clinical Chemistry, In Methods in Enzymology, ed. L. Brand, M. L. Johnson.
Ried, T., A. Baldini, T.C. Rand, D.C. Ward. (1992) Simultaneous visualization of seven different DNA probes by in situ hybridization using combinatorial fluorescence and digital imaging microscopy. Proc. Natl. Acad. Sci. 89:1388–1392.
Gadella, T.W.J., T.M. Jovin, R.M. Clegg. (1993) Fluorescence Lifetime Imaging Microscopy (FLIM) - Spatial Resolution Of Microstructures On The Nanosecond Time Scale. Biophysical Chem. 48:221–239.
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Selvin, P.R. (1999). Luminescent Lanthanide Chelates for Improved Resonance Energy Transfer and Application to Biology. In: Applied Fluorescence in Chemistry, Biology and Medicine. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-59903-3_19
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DOI: https://doi.org/10.1007/978-3-642-59903-3_19
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