Abstract
In light of important implication of fibrinogen and resveratrol in the platelet aggregation and thrombus formation, the interaction between them was studied, and its biological implication was further explained. Fibrinogen could interact with resveratrol to form 1:1 complex with the binding constant of 1.11 × 104 M−1. The binding was spontaneous and fibrinogen/resveratrol complex formation was an exothermal reaction. Electronic interaction and hydrogen bonding played key roles and non-radiation energy transferred from fibrinogen to resveratrol in the binding process. Kinetic study indicated that resveratrol linearly combined to fibrinogen along with the prolonged time. The addition of resveratrol changed fibrinogen conformation including its second structure resulting in increase of polarity around tyrophore residue and decrease of α-helical structure in the protein. Additionally, fibrinogen obviously increased resveratrol stability. It would give a deeper insight into resveratrol as a kind of functional factor.
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