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Luminescent spectral properties of rhodamine derivatives while binding to serum albumin

Luminescent spectral properties of rhodamine derivatives while binding to serum albumin,10.1007/s10812-006-0095-z,Journal of Applied Spectroscopy,N. N

Luminescent spectral properties of rhodamine derivatives while binding to serum albumin   (Citations: 1)
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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.
Journal: Journal of Applied Spectroscopy - J APPL SPECTROSC , vol. 73, no. 3, pp. 432-436, 2006
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    • ...Earlier the interaction of rhodamine [12] squaraine [13] and styrylcyanine dyes on the base of F-dye (4 - (4 - (dimethylamino)styryl)-1-methylpyridinium iodide) with BSA and deoxyribonucleic acid [15] was studied...
    • ...At this, part of the non-polar molecules of detergent would be associated with the hydrophobic centres of adsorption of proteins and thereby inhibit the interaction of proteins with the dye molecules [12]...

    Eldar N. Kurtaliev. Spectroscopic Study of the Interaction of Styrylcyanine Dyes Sbo, Sil ...

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