Luminescent spectral properties of rhodamine derivatives while binding to serum albumin View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2006-05

AUTHORS

N. Nizomov, Z. F. Ismailov, É. N. Kurtaliev, Sh. N. Nizamov, G. Khodzhaev, L. D. Patsenker

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. More... »

PAGES

432-436

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s10812-006-0095-z

DOI

http://dx.doi.org/10.1007/s10812-006-0095-z

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1051474494


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