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Journal of Applied Spectroscopy

, Volume 86, Issue 5, pp 855–860 | Cite as

Effect of the Association of Eosin Molecules on Their Interaction with Bovine Serum Albumin at Various pH Values

  • E. S. Gorodnichev
  • A. A. Kuleshova
  • A. V. Bykov
  • A. M. SaletskyEmail author
Article
  • 3 Downloads

The fluorescence characteristics of eosin in solutions of bovine serum albumin (BSA) were studied at various pH. The quenching of eosin fluorescence with increasing concentration was found to result from two competing processes: binding of BSA molecules with eosin molecules and the formation of associated species of the dye. The extent of association as well as the structural and thermodynamic parameters of eosin were determined in buffer and BSA solutions at different pH. Variation of the buffer solution pH led to change of these characteristics. The effect of the formation of associated species of eosin in BSA solutions on the dynamic quenching constant of eosin fluorescence was examined. The formation of associated species of eosin was shown to lead to a decrease in the dynamic quenching constant of this dye, which is proportional to the pH of the solution.

Keywords

eosin bovine serum albumin dimer extent of association dimer structure enthalpy of dissociation fluorescence quenching dynamic fluorescence quenching constant 

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© Springer Science+Business Media, LLC, part of Springer Nature 2019

Authors and Affiliations

  • E. S. Gorodnichev
    • 1
  • A. A. Kuleshova
    • 1
  • A. V. Bykov
    • 1
  • A. M. Saletsky
    • 1
    Email author
  1. 1.M. V. Lomonosov Moscow State UniversityMoscowRussia

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