Investigation of the association behaviors between biliverdin and bovine serum albumin by fluorescence spectroscopy

Yan li Wei, Jian qing Li, Chuan Dong*, Shao min Shuang, Dian sheng Liu, Carmen W K HUIE

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

113 Citations (Scopus)

Abstract

The interaction between biliverdin and bovine serum albumin (BSA) has been studied by steady fluorescence spectroscopy, synchronous fluorescence and resonance light scanning spectra. The binding of biliverdin to BSA quenches the tryptophan residue fluorescence and the results show that both static and dynamic quenching occur together with complex formation. The binding constant and binding sites of biliverdin to BSA at pH 7.1 are calculated to be 3.33 × 108 L/mol and 1.54, respectively, according to the double logarithm regression curve. In addition, the distance between the biliverdin and BSA is estimated to be 1.25 nm using Föster's equation on the basis of the fluorescence energy transfer. Furthermore the synchronous fluorescence spectra show that the microenvironment of the tryptophan residues has not obvious changes, which obeys the phase distribution model. Finally, the thermodynamic data show that biliverdin molecules enter the hydrophobic cavity of BSA via hydrophobic interaction.

Original languageEnglish
Pages (from-to)377-382
Number of pages6
JournalTalanta
Volume70
Issue number2
DOIs
Publication statusPublished - 15 Sep 2006

Scopus Subject Areas

  • Analytical Chemistry

User-Defined Keywords

  • Biliverdin
  • Bovine serum albumin
  • Tryptophan fluorescence quenching spectroscopy

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