Resveratrol binding to collagen and its biological implication

Considering important implication of collagen and resveratrol in platelet aggregation and cancer metastasis, interaction between them and its biological significance were studied. Resveratrol could interact with collagen to form a 1:1 complex with a binding constant at about 105 M−1. It decreased fluorescence emission intensities of tyrosine, improved the formation of excimer-like species and dityrosine, and had no effect on post-translational, chemical, age-related modifications in the resveratrol/collagen solution. The binding process was spontaneous and the formation was an exothermic reaction. Thermodynamic analysis suggests that both hydrophobic interaction and hydrogen bonding played key roles in the course of resveratrol–collagen binding. Moreover, synchronous fluorescence and FT-IR results indicate that the interaction caused decrease of the polarity around tyrosine residues resulting in collagen conformation alteration. Additionally, the isomerisation of resveratrol was not prevented but its stability was improved with the addition of collagen in the solution. This work might provide a more comprehensive understanding about the anticancer and antiplatelet activities of resveratrol as a functional food factor.

► Resveratrol could interact with collagen to form a 1:1 complex.
► The binding process was spontaneous.
► Hydrophobic interaction played a key role in the process of the binding.
► The interaction effect caused collagen conformation alteration.
► The stability of resveratrol was improved with the addition of collagen.