Luminescent spectral properties of rhodamine derivatives while binding to serum albumin |
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Authors: | N Nizomov Z F Ismailov É N Kurtaliev Sh N Nizamov G Khodzhaev L D Patsenker |
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Institution: | (1) Samarkand State University, 15 Universitetskii bul’v., Samarkand, 703004, Uzbekistan;(2) Samarkand Agricultural Institute, Uzbekistan;(3) Institute of Scintillation Materials, National Academy of Sciences of Ukraine, Kharkov |
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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.
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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Keywords: | rhodamine dyes fluorescence serum albumin binding constant effect of temperature |
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