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Published on: January 28, 2013
Resveratrol binding to human serum albumin
C N N' soukpoe-Kossi1, C St-Louis, M Beauregard
1Département de Chimie-biologie, Université du Québec à Trois-Rivières, C. P. 500, Trois-Rivières, Québec, G9A 5H7, Canada.
Journal of Biomolecular Structure & Dynamics
|October 24, 2006
Summary
Resveratrol binds to human serum albumin (HSA) through hydrogen bonding. High concentrations of resveratrol partially stabilize HSA
Area of Science:
- Biochemistry
- Molecular Biology
- Pharmacology
Background:
- Resveratrol (Res) is a polyphenol found in red grapes and wine.
- Resveratrol exhibits pharmaceutical properties, including cardiovascular benefits.
- It binds proteins and inhibits enzymes like cyclooxygenase.
Purpose of the Study:
- To investigate the interaction between resveratrol and human serum albumin (HSA).
- To determine the binding mode, constant, and structural effects of resveratrol on HSA.
Main Methods:
- Utilized FTIR, UV-Visible, Circular Dichroism (CD), and fluorescence spectroscopy.
- Employed constant protein concentration (0.3 mM) with varying resveratrol concentrations (μM to mM).
Main Results:
- Resveratrol binds non-specifically to HSA via hydrogen bonding with a binding constant of 2.56 x 10^5 M⁻¹.
- Low resveratrol concentrations showed no significant structural changes in HSA.
- High resveratrol concentrations (1 mM) increased alpha-helix content from 57% to 62% and decreased beta-sheet from 10% to 7%.
Conclusions:
- Resveratrol interacts with HSA through hydrogen bonds.
- High resveratrol concentrations induce partial stabilization of HSA's secondary structure, favoring alpha-helical content.
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