Resveratrol Binding to Human Serum Albumin

• Published in: Journal of biomolecular structure & dynamics Vol. 24; no. 3; pp. 277 - 283
• Main Authors: N′ soukpoé-Kossi, C. N., St-Louis, C., Beauregard, M., Subirade, M., Carpentier, R., Hotchandani, S., Tajmir-Riahi, H. A.
• Format: Journal Article
• Language: English
• Published: England Taylor & Francis Group 01-12-2006
• Subjects: Angiogenesis Inhibitors - pharmacokinetics; Binding constant; Binding mode; Binding Sites; Circular Dichroism; Fluorescence spectroscopy; FTIR; Humans; Models, Molecular; Protein; Protein Binding; Protein Conformation; Protein Structure, Secondary; Resveratrol; Secondary structure; Serum Albumin - chemistry; Serum Albumin - metabolism; Spectroscopy, Fourier Transform Infrared; Stilbenes - pharmacokinetics; UV-Vis
• ISSN: 0739-1102; 1538-0254
• DOI: 10.1080/07391102.2006.10507120

Resveratrol (Res), a polyphenolic compound found largely in the skin of red grape and wine, exhibits a wide range of pharmaceutical properties and plays a role in prevention of human cardiovascular diseases [Pendurthi et al., Arterioscler. Thromb. Vasc. Biol. 19, 419-426 (1999)]. It shows a strong affinity towards protein binding and used as inhibitor for cyclo- oxygenase and ribonuclease reductase. The aim of this study was to examine the interaction of resveratrol with human serum albumin (HSA) in aqueous solution at physiological conditions, using a constant protein concentration (0.3 mM) and various pigment contents μM to mM). FTIR, UV-Visible, CD, and fluorescence spectroscopic methods were used to determine the resveratrol binding mode, the binding constant and the effects of pigment complexation on protein secondary structure.
Structural analysis showed that resveratrol bind non-specifically (H-bonding) via polypeptide polar groups with overall binding constant of K
Res
= 2.56× 10
5
M
−1
. The protein secondary structure, analysed by CD spectroscopy, showed no major alterations at low resveratrol concentrations (0.125 mM), whereas at high pigment content (1 mM), major increase of α-helix from 57% (free HSA) to 62% and a decrease of β-sheet from 10% (free HSA) to 7% occurred in the resveratrol-HSA complexes. The results indicate a partial stabilization of protein secondary structure at high resveratrol content.