Probing the binding of procyanidin B3 to human serum albumin by isothermal titration calorimetry

• Procyanidin B3-HSA system is driven by favorable enthalpy and unfavorable entropy.
• Hydrogen bond and van der Waals force are the major binding forces.
• The binding constant for procyanidin B3 with HSA is in the intermediate range.
• The equilibrium fraction of unbound procyanidin B3 fu > 90%.
• Procyanidin B3 can be stored and carried by serum albumin to reach its target organ.

Proanthocyanidins are a mixture of monomers, oligomers, and polymers of flavan-3-ols that are widely distributed in the plant kingdom. One of the most widely studied proanthocyanidins is procyanidin B3. In this study, the interaction between procyanidin B3 and human serum albumin (HSA) was investigated using isothermal titration calorimetry (ITC). Thermodynamic investigations reveal that the hydrogen bond and van der Waals force are the major binding forces in the binding of procyanidin B3 to HSA. The binding of procyanidin B3 to HSA is driven by favorable enthalpy and unfavorable entropy. The obtained binding constant for procyanidin B3 with HSA is in the intermediate range and the equilibrium fraction of unbound procyanidin B3 fu > 90% at the physiological concentration of HSA shows that procyanidin B3 can be stored and transported from the circulatory system to reach its target site. The stoichiometric binding number n approximately equals to 1, suggesting that one molecule of procyanidin B3 combines with one molecule of HSA and no more procyanidin B3 binding to HSA occurs at the concentration used in this study.

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