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Abstrakty
The particles of Congo red (CR), a bis-azo dye, associate in aqueous solutions, forming ribbon-like micelles. Supramolecular dyes, as a result of their molecular size, have a limited capability of penetrating into the interior of the majority of native proteins and do not enter living cells surrounded by an intact phospholipid membrane. They may however, bind to proteins with structure destabilized by unfolding (during denaturation) or function-related changes (e.g. surface cell receptors). Congo red absorbs visible light with a maximum absorption at 500 nm, in aqueous solutions at neutral pH. After CR bind to the polymers (such as cellulose) or certain proteins, dye’s behaviour changes remarkably. These binding affects spectral properties of the dye: the absorption spectrum of the Congo red shifts towards longer wavelengths and receives a yellow-red fluorescence. A numerical analysis of the graphic data obtained from fluorescent microscope (division into channels corresponding to constituent colours and with the noise separated using a graphical program) allowed to understand better the causes of movement of the CR fluorescence spectrum and to identify the properties of substances associating with the CR micelle. By means of a statistical analysis of the data it was possible to observe that wavelength of emission and intensity of fluorescence is not only associated with the polarity of the environment but mainly with the strength of the association between the Congo red micelle and the matrix.
Słowa kluczowe
Czasopismo
Rocznik
Tom
Strony
17--23
Opis fizyczny
Bibliogr. 29 poz., tab., wykr., zdj.
Twórcy
autor
- Chair of Medical Biochemistry, Medical College, Jagiellonian University, Kopernika 7, 31-034 Krakow, Poland
autor
- Chair of Medical Biochemistry, Medical College, Jagiellonian University, Kopernika 7, 31-034 Krakow, Poland
autor
- Chair of Medical Biochemistry, Medical College, Jagiellonian University, Kopernika 7, 31-034 Krakow, Poland
autor
- Chair of Medical Biochemistry, Medical College, Jagiellonian University, Kopernika 7, 31-034 Krakow, Poland
autor
- Chair of Medical Biochemistry, Medical College, Jagiellonian University, Kopernika 7, 31-034 Krakow, Poland
autor
- Chair of Medical Biochemistry, Medical College, Jagiellonian University, Kopernika 7, 31-034 Krakow, Poland
Bibliografia
- 1. Roterman I., No K.T., Piekarska B., Kaszuba J., Pawlicki R., Rybarska J., Konieczny L.: Bis azo dyes - studies on the mechanism of complex formation with IgG modulated by heating or antigen binding. J Physiol Pharmacol. 1993; 44(3): 213-232.
- 2. Stopa B., Konieczny L., Piekarska B., Roterman I., Rybarska J., Skowronek M.: Effect of self association of bis-ANS and bis-azo dyes on protein binding. Biochimie. 1997; 79(1): 23-26.
- 3. Stopa B., Piekarska B., Konieczny L., Rybarska J., Spolnik P., Zemanek G., Roterman I., Krol M.: The structure and protein binding of amyloid-specific dye reagents. Acta Biochim. Pol. 2003; 50(4): 1213-1227.
- 4. Glenner G.G., Eanes E.D., Page D.L.: The relation of the properties of Congo red-stained amyloid fibrils to the conformation. J Histochem. Cytochem. 1972; 20(10): 821-826.
- 5. Roterman I., Krol M., Nowak M., Konieczny L., Rybarska J., Stopa B., Piekarska B., Zemanek G.: Why Congo red binding is specific for amyloid proteins - model studies and a computer analysis approach. Med. Sci. Monit. 2001; 7(4): 771-784.
- 6. Rybarska J., Konieczny L., Piekarska B., Stopa B., Roterman I.: The detection of specific acute phase serum protein complexes and immune complexes by Congo red binding. J. Physiol. Pharmacol. 1995; 46(2): 221-231.
- 7. Pepys M.B.: Pathogenesis, diagnosis and treatment of systemic amyloidosis. Philos. Trans. R. Soc. Lond. B. Biol. Sci. 2001; 356(1406): 203-210.
- 8. Kaszuba J., Konieczny L., Piekarska B., Rotterman I., Rybarska J. Bis-azo dyes interference with effector activation of antibodies. J. Physiol. Pharmacol. 1993; 44(3): 233-242.
- 9. Piekarska B., Roterman I., Rybarska J., Konieczny L., Kaszuba J.: The melting of native domain structure in effector activation of IgG studied by using Congo red as a specific probe. J. Physiol. Pharmacol. 1994; 45(1): 147-162.
- 10. Piekarska B., Rybarska J., Stopa B., Zemanek G., Krol M., Roterman I., Konieczny L.: Supramolecularity creates nonstandard protein ligands. Acta Biochim. Pol. 1999; 46(4): 841-851.
- 11. Rybarska J., Konieczny L., Roterman I., Piekarska B.: The effect of azo dyes on the formation of immune complexes. Arch. Immunol. Ther. Exp. (Warsz.). 1991; 39(3): 317-327.
- 12. Zemanek G., Rybarska J., Stopa B., Piekarska B., Spolnik P., Konieczny L., Roterman I., Bugajski A.: Protein distorsion-derived mechanism of signal discrimination in monocytes revealed using Congo red to stain activated cells. Folia Histochem. Cytobiol. 2003; 41(3): 113-124.
- 13. Ding F., Li N., Han B., Liu F., Zhang L., Sun Y.: The binding of C.I. acid red 2 to human serum albumin: Determination of binding mechanism and binding site using fluorescence spectroscopy. Dyes and Pigments. 2009; 83(2): 249-257.
- 14. Yilmaz E., Memon S., Yilmaz M.: Removal of direct azo dyes and aromatic amines from aqueous solutions using two beta-cyclodextrin-based polymers. J. Hazard. Mater. 2010; 174(1-3): 592-597.
- 15. Lorenc-Grabowska E., Gryglewicz G.: Adsorption characteristics of Congo red on coal-based mesoporous activated carbon. Dyes and Pigments. 2007; 74(1): 34-40.
- 16. Briggs C., Burgin S.: Congo red, an effective stain for revealing the chytrid fungus, batrachochytrium dendrobatidis, in epidermal skin scrapings from frogs. Mycologist 2004; 18(3): 98-103.
- 17. Nilsson K.P.R.: Small organic probes as amyloid specific ligands – past and recent molecular scaffolds. FEBS Lett. 2009; 583(16): 2593-2599.
- 18. Eisert R., Felau L., Brown L.R.: Methods for enhancing the accuracy and reproducibility of Congo red and thioflavin T assays. Anal. Biochem. 2006; 353(1): 144-146.
- 19. Klunk W.E, Debnath M.L, Pettegrew J.W.: Chrysamine-G binding to alzheimer and control brain: Autopsy study of a new amyloid probe. Neurobiol. Aging. 1995; 16(4): 541-548.
- 20. Klunk W.E, Pettegrew J.W, Abraham D.J.: Quantitative evaluation of Congo red binding to amyloid-like proteins with a beta-pleated sheet conformation. J. Histochem. Cytochem. 1989; 37(8): 1273-1281.
- 21. Cooper J.H.: Selective amyloid staining as a function of amyloid composition and structure. Histochemical analysis of the alkaline Congo red, standardized toluidine blue, and iodine methods. Lab. Invest. 1974; 31(3): 232-238.
- 22. Glenner G.G, Eanes E.D, Page D.L.: The relation of the properties of Congo red-stained amyloid fibrils to the -conformation. J. Histochem. Cytochem. 1972; 20(10): 821-826.
- 23. Pigorsch E., Elhaddaoui A., Turrell S.: Spectroscopic study of pH and solvent effects on the structure of Congo red and its binding mechanism to amyloid-like proteins. Spectrochim. Acta, Pt A: Mol. Spectrosc. 1994; 50(12): 2145-2152.
- 24. Kowalczyk A.: Biospektroskopia. Twardowski J. Ed.; Vol. 3; PWN; Warszawa 1989, pp. 9-67.
- 25. Shukla A., Mukherjee S., Sharma S., Agrawal V., Radha Kishan K.V., Guptasarma P.: A novel UV laser-induced visible blue radiation from protein crystals and aggregates: Scattering artifacts or fluorescence transitions of peptide electrons delocalized through hydrogen bonding? Arch. Biochem. Biophys. 2004; 428(2): 144-153.
- 26. Linke R.P.: Highly sensitive diagnosis of amyloid and various amyloid syndromes using Congo red fluorescence. Virchows Arch. 2000; 436(5): 439-448.
- 27. Zhang Y., Xiang X., Mei P., Dai J., Zhang L., Liu Y.: Spectroscopic studies on the interaction of Congo red with bovine serum albumin. Spectrochim. Acta, Pt A: Mol. Spectrosc. 2009; 72(4): 907-914.
- 28. Nekipelova T.D, Shishkov V.S.: Solvent effect on the spectral characteristics and quantum yields of the photolysis of alkylated 1,2-dihydroquinolines. High Energy Chemistry 2004; 38(5): 315-322.
- 29. Wang Z.P., Zhang Z.M., Ding Z.J.: Photoluminescence study of Congo red molecules under high pressure. J. Lumin. 2007;122(123): 237-240.
Typ dokumentu
Bibliografia
Identyfikator YADDA
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