Fluorescence spectroscopy was used to investigate the interaction between resveratrol and whey proteins. The whey proteins examined were lactoferrin, holo-lactoferrin, apo-lactoferrin, whey protein isolate (WPI) and the β-lactoglobulin- and α-lactalbumin-rich fractions of WPI. Both an analytical-grade and food-grade resveratrol were examined. In all the systems studied, it was found that resveratrol interacted with the whey proteins to form a 1:1 complex. The binding constant, Ks, for the protein–resveratrol complex for all the proteins examined varied from 1.7 × 104 to 1.2 × 105 m−1. Furthermore, the interaction between the whey proteins and resveratrol did not affect the secondary structure of the proteins.