Flavonoid binding to human serum albumin

Alessandro Bolli, Maria Marino, Gerald Rimbach, Gabriella Fanali, Mauro Fasano, Paolo Ascenzi

Research output: Contribution to journalArticle

Abstract

Dietary flavonoid may have beneficial effects in the prevention of chronic diseases. However, flavonoid bioavailability is often poor probably due to their interaction with plasma proteins. Here, the affinity of daidzein and daidzein metabolites as well as of genistein, naringenin, and quercetin for human serum albumin (HSA) has been assessed in the absence and presence of oleate. Values of the dissociation equilibrium constant (K) for binding of flavonoids and related metabolites to Sudlow's site I range between 3.3×10-6 and 3.9×10-5M, at pH 7.0 and 20.0°C, indicating that these flavonoids are mainly bound to HSA in vivo. Values of K increase (i.e., the flavonoid affinity decreases) in the presence of saturating amounts of oleate by about two folds. Present data indicate a novel role of fatty acids as allosteric inhibitors of flavonoid bioavailability, and appear to be relevant in rationalizing the interference between dietary compounds, food supplements, and drugs.

Original languageEnglish
Pages (from-to)444-449
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume398
Issue number3
DOIs
Publication statusPublished - Jul 2010

    Fingerprint

Keywords

  • Allostery
  • Daidzein
  • Daidzein metabolites
  • Flavonoid binding
  • Genistein
  • Human serum albumin
  • Naringenin
  • Oleate
  • Quercetin
  • Thermodynamics

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Molecular Biology

Cite this

Bolli, A., Marino, M., Rimbach, G., Fanali, G., Fasano, M., & Ascenzi, P. (2010). Flavonoid binding to human serum albumin. Biochemical and Biophysical Research Communications, 398(3), 444-449. https://doi.org/10.1016/j.bbrc.2010.06.096