Luminescent spectral properties of rhodamine derivatives while binding to serum albumin

Nizomov, N.; Ismailov, Z. F.; Kurtaliev, É. N.; Nizamov, Sh. N.; Khodzhaev, G.; Patsenker, L. D.
May 2006
Journal of Applied Spectroscopy;May2006, Vol. 73 Issue 3, p432
Academic Journal
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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