Luminescent spectral properties of rhodamine derivatives while binding to serum albumin

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

Research output: Contribution to journalArticlepeer-review

12 Scopus citations


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.

Original languageEnglish
Pages (from-to)432-436
Number of pages5
JournalJournal of Applied Spectroscopy
Issue number3
StatePublished - May 2006
Externally publishedYes


  • Binding constant
  • Effect of temperature
  • Fluorescence
  • Rhodamine dyes
  • Serum albumin


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