Abstract
We have studied the effect of blood serum albumin on the absorption and fluorescence spectra of rhodamine C (RC), rhodamine 6G (R6G), and rhodamine 3B (R3B). Interaction of the dye with protein is assessed using the binding parameters: binding constants and concentrations of binding sites. We have studied the effect of temperature on the binding parameters. We have observed that heating a mixture of the dye solution with protein for 30 min leads to an increase in the binding constant for rhodamine 3B with protein by a factor of 2, while the concentration of binding sites increases by a factor of 2.3. This is explained by features of the globular protein structure and a change in its conformation when heated. We have shown that rhodamine 3B at a concentration of 10−5 M is the most effective among the studied rhodamine dyes for application as a fluorescent probe when studying conformational changes in blood serum protein.
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Report given at the Third International Conference on Liquid State Physics: Current Problems, May 27–31, 2005, Kiev, Ukraine.
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Translated from Zhurnal Prikladnoi Spektroskopii, Vol. 73, No. 3, pp. 380–384, May–June, 2006.
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Nizomov, N., Ismailov, Z.F., Kurtaliev, É.N. et al. Luminescent spectral properties of rhodamine derivatives while binding to serum albumin. J Appl Spectrosc 73, 432–436 (2006). https://doi.org/10.1007/s10812-006-0095-z
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DOI: https://doi.org/10.1007/s10812-006-0095-z