Fluorescence Correlation Analysis for Diagnosis Based on Molecular Dynamics

Yasutomo Nomura^1,

¹Department of Systems Life Engineering, Maebashi Institute of Technology, Kamisadori, Maebashi, Japan

Cite this paper:
Yasutomo Nomura. Fluorescence Correlation Analysis for Diagnosis Based on Molecular Dynamics. Biomedical Science and Engineering. 2016; 4(1):23-30. doi: 10.12691/bse-4-1-3

Abstract

Fluorescence correlation spectroscopy is a powerful method in clinical laboratory where a lot of samples of patients will be determined because it enables to measure concentration and molecular weight of tested molecules without any physical separation steps. Nevertheless it may not yet be used as widely as one expected. The reason is that it is likely to be difficult for many users to understand the theoretical background. In this method, the users measured intensity fluctuation of fluorescence resulted from the molecules entering and exiting tiny volume element, namely Brownian motion in solution. Using the time series data of fluorescence intensity, the autocorrelation function was calculated. When the function was fit to the analytical model derived from diffusion theory, concentration and molecular weight of fluorophores were obtained. This minireview described the theoretical background of Brownian motion, physical meaning of the correlation analysis, and its usage properly dependent on samples from homogeneous solution to inhomogeneous cell. Furthermore the recent advances are also outlined.

Keywords:
fluorescence correlation spectroscopy Brownian motion diffusion theory diagnosis clinical laboratory

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References:

[1]	Gourley, G.A., and Duncan, D.V., “Patient satisfaction and quality of life humanistic outcomes,” The American Journal of Managed Care, 4(5). 746-752. May 1998.
[2]	Poley, M.J., “Nutrition and health technology assessment: when two worlds meet,” Frontiers in Pharmacology, 6. 232. Oct. 2015.
[3]	Lakowicz J., Principles of Fluorescence Spectroscopy, Springer, 2006.
[4]	Einstein, A., Investigations on the theory of the Brownian movement, Dover Publications, NY, 1956.
[5]	Magde, D., Elson, E.L., and Webb, W.W., “Fluorescence correlation spectroscopy. II. An experimental realization,” Biopolymers, 13(1). 29-61. Jan. 1974.
[6]	Weissman, M., Schindler, H., and Feher, G., “Determination of molecular weights by fluctuation spectroscopy: application to DNA,” Proceedings of the National Academy of Sciences of the United States of America, 73(8). 2776-2780. Aug. 1976.
[7]	Eigen, M. and Rigler, R., “Sorting single molecules: application to diagnostics and evolutionary biotechnology,” Proceedings of the National Academy of Sciences of the United States of America, 91(13). 5740-5747. Jun. 1994.
[8]	Kinjo, M. and Rigler, R., “Ultrasensitive hybridization analysis using fluorescence correlation spectroscopy,” Nucleic Acids Research, 23(10). 1795-1799. May 1995.
[9]	Nomura, Y., Fuchigami, H., Kii, H., Feng, Z., Nakamura, T., et al., “Detection of oxidative stress-induced mitochondrial DNA damage using fluorescence correlation spectroscopy,” Analytical Biochemistry, 350(2). 196-201. Mar. 2006.
[10]	Nomura, Y., Fuchigami, H., Kii, H., Feng, Z., Nakamura, T., et al., “Quantification of size distribution of restriction fragments in mitochondrial genome using fluorescence correlation spectroscopy,” Experimental and Molecular Pathology, 80(3). 275-278. Jun. 2006.
[11]	Nomura, Y. and Kinjo, M., “Real-time monitoring of in vitro transcriptional RNA by using fluorescence correlation spectroscopy,” ChemBioChem, 5(12). 1701-1703. Dec. 2004.
[12]	Nomura, Y., Tanaka, H., Poellinger, L., Higashino, F., and Kinjo, M., “Monitoring of in vitro and in vivo translation of green fluorescent protein and its fusion proteins by fluorescence correlation spectroscopy,” Cytometry, 44(1). 1-6. May 2001.
[13]	Foldes-Papp, Z., Kinjo, M., Tamura, M., Birch-Hirschfeld, E., Demel, U., et al., “A new ultrasensitive way to circumvent PCR-based allele distinction: direct probing of unamplified genomic DNA by solution-phase hybridization using two-color fluorescence cross-correlation spectroscopy,” Experimental and Molecular Pathology, vol. 78(3). 177-189. Jun. 2005.
[14]	Sun, F., Mikuni, S., and Kinjo, M., “Monitoring the caspase cascade in single apoptotic cells using a three-color fluorescent protein substrate,” Biochemical and Biophysical Research Communications, 404(2). 706-710. Jan. 2011.
[15]	Kolin, D.L. and Wiseman, P.W., “Advances in image correlation spectroscopy: measuring number densities, aggregation states, and dynamics of fluorescently labeled macromolecules in cells,” Cell Biochemistry and Biophysics, 49(3). 141-164. Oct. 2007.
[16]	Nomura, Y., “Direct quantification of mitochondria and mitochondrial DNA dynamics,” Current Pharmaceutical Biotechnology, 13(14). 2617-2622. Nov. 2012.
[17]	Fujii F. and Kinjo, M., “Detection of antigen protein by using fluorescence cross-correlation spectroscopy and quantum-dot-labeled antibodies,” ChemBioChem, 8(18). 2199-2203. Dec. 2007.
[18]	Klapper, Y., Maffre, P., Shang, L., Ekdahl, K.N., Nilsson, B., et al., “Low affinity binding of plasma proteins to lipid-coated quantum dots as observed by in situ fluorescence correlation spectroscopy,” Nanoscale, 7(22). 9980-9984. Jun. 2015.
[19]	Edman, L., Mets, U., and Rigler, R., “Conformational transitions monitored for single molecules in solution,” Proceedings of the National Academy of Sciences of the United States of America, 93(13). 6710-6715. Jun. 1996.
[20]	Meseth, U., Wohland, T., Rigler, R., and Vogel, H., “Resolution of fluorescence correlation measurements,” Biophysical Journal, 76(3). 1619-1631. Mar. 1999.
[21]	Fujii, F., Horiuchi, M., Ueno, M., Sakata, H., Nagao, I., et al., “Detection of prion protein immune complex for bovine spongiform encephalopathy diagnosis using fluorescence correlation spectroscopy and fluorescence cross-correlation spectroscopy,” Analytical Biochemistry, 370(2). 131-141. Nov. 2007.
[22]	Schwille, P., Meyer-Almes, F.J., and Rigler, R., “Dual-color fluorescence cross-correlation spectroscopy for multicomponent diffusional analysis in solution,” Biophysical Journal, 72(4). 1878-1886. Apr. 1997.
[23]	Kogure, T., Karasawa, S., Araki, T., Saito, K., Kinjo, M., et al., “A fluorescent variant of a protein from the stony coral Montipora facilitates dual-color single-laser fluorescence cross-correlation spectroscopy,” Nature Biotechnology, 24(5). 577-581. May 2006.
[24]	Nomura, Y. and Kinjo, M., “Editorial: Current optical procedures used in cell biology,” Current Pharmaceutical Biotechnology, 13(14). 2545-2546. Nov. 2012.
[25]	Matsuo, T., Nakayama, K., Nishimoto, K., and Nomura, Y., “Image Processing Methods for Quantitative Analysis of Mitochondrial DNA Dynamics,” Biochemistry and Analytical Biochemistry, S3-001. 2012.
[26]	Digman, M.A. and Gratton, E., “Analysis of diffusion and binding in cells using the RICS approach,” Microscopy Research and Technique, 72(4). 323-332. Apr. 2009.
[27]	Wiseman, P.W., Squier, J.A., Ellisman, M.H., and Wilson, K.R., “Two-photon image correlation spectroscopy and image cross-correlation spectroscopy,” Journal of Microscopy, 200(1). 14-25. Oct. 2000.
[28]	Pozzi, P., Sironi, L., D'Alfonso, L., Bouzin, M., Collini, M., et al., “Electron multiplying charge-coupled device-based fluorescence cross-correlation spectroscopy for blood velocimetry on zebrafish embryos,” Journal of Biomedical Optics, 19(6). 067007. Jun. 2014.
[29]	Goto, T., Sato, M., Takahashi, E., and Nomura, Y., “Image analysis of colocalization of nuclear DNA and GFP labelled HIF-1alpha in stable transformants,” Current Pharmaceutical Biotechnology, 13(14). 2547-2550. Nov. 2012.