Compared binding properties between resveratrol and other polyphenols to plasmatic albumin: consequences for the health protecting effect of dietary plant microcomponents

• Published in: Molecules (Basel, Switzerland) Vol. 19; no. 11; pp. 17066 - 17077
• Main Authors: Latruffe, Norbert, Menzel, Matthias, Delmas, Dominique, Buchet, René, Lançon, Allan
• Format: Journal Article Book Review
• Language: English
• Published: Switzerland MDPI AG 24-10-2014; MDPI
• Subjects: affinity; Binding Sites - physiology; Biochemistry; Biochemistry, Molecular Biology; Diet - methods; Flavonoids - metabolism; fluorescence; Food; Health; Humans; Life Sciences; Plants, Edible - metabolism; Polyphenols - metabolism; quercetin; Resveratrol; Review; Serum Albumin - metabolism; Stilbenes - metabolism; structural changes
• ISSN: 1420-3049; 1420-3049
• DOI: 10.3390/molecules191117066

Phytophenols are considered to have beneficial effects towards human physiology. They are food microcomponents with potent chemopreventive properties towards the most three frequent contemporary human diseases, e.g., cardiovascular alterations, cancer and neurodegenerative pathologies. Related to this, the plasmatic form and plasmatic level of plant polyphenols in the body circulation are crucial for their efficiency. Thus, determinations of the binding process of resveratrol and of common flavonoids produced by major edible plants, berries and fruits to plasma proteins are essential. The interactions between resveratrol and albumin, a major plasma protein, were compared with those already published, involving curcumin, genistein, quercetin and other well-known food-containing polyphenols. The approaches used are usually intrinsic fluorescence intensity changes, quenching of protein intrinsic fluorescence and infrared spectroscopy. It appears that: (1) all of the studied polyphenols interact with albumin; (2) while most of the studied polyphenols interact at one albumin binding site, there are two different types of resveratrol binding sites for bovine serum albumin, one with the highest affinity (apparent KD of 4 µM) with a stoichiometry of one per monomer and a second with a lower affinity (apparent KD of 20 µM) with also a stoichiometry of one per monomer; (3) at least one binding site is in the vicinity of one tryptophanyl residue of bovine serum albumin; and (4) resveratrol binding to bovine serum albumin produces a very small structural conformation change of the polypeptide chain. These results support a role played by polyphenols-albumin interactions in the plasma for the bio-activities of these food microcomponents in the body.