Resveratrol and fibrinogen interactions

Abstract

The French paradox describes a lower incidence of cardiovascular problems despite a high intake of saturated fats. This phenomenon was associated with higher consumption of red wine, only to be later discovered that the presence of several antioxidants, including resveratrol, are responsible for it. We investigated if resveratrol has a more direct role in protection from harmful oxidation and development of thrombosis, presumably through binding to important proteins of the blood coagulation process. Spectrofluorimetric analysis demonstrated binding of resveratrol to fibrinogen, the main protein in the coagulation process, which also has an important application as a food additive in making of fibrin gels. Various spectroscopic methods have demonstrated that binding of resveratrol does not unfold or destabilize fibrinogen since both near and far-UV CD spectra as well as its melting temperature remained unchanged. A mutuallyprotective effect against the free radical- induced oxidation of resveratrol and fibrinogen was found. The presence of fibrinogen caused a very small masking effect of the antioxidative potential of resveratrol, measured by a reduction of hexacyanoferrate (III), while greatly increasing its solubility in an aqueous environment, thus increasing potential bioavailability and activity of resveratrol in circulation. By direct interaction and protection of fibrinogen, resveratrol may serve as an important antioxidant for prevention of thrombosis. The antioxidative effect of resveratrol may also protect and thus keep the desired characteristics of fibrinogen during the application of this protein as a food additive.