Flavonoid binding to human serum albumin

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

Research output: Contribution to journalArticlepeer-review


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
Issue number3
Publication statusPublished - Jul 2010


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

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Molecular Biology

Fingerprint Dive into the research topics of 'Flavonoid binding to human serum albumin'. Together they form a unique fingerprint.

Cite this