Stability of trans-resveratrol associated with transport proteins.

Spectrophotometry and fluorescence combined with docking and molecular dynamics simulations are used to study the effect of the carrier proteins β-lactoglobulin and human serum albumin on the degradative trans-to-cis conversion of resveratrol. The spectroscopic measurements quantify the concentration of resveratrol isoforms after 2 h of irradiation with light at 340 nm, showing that their ratio depends linearly on temperature between 20 and 50 °C and obeys an Arrhenius law with activation energies of photoisomerization of 7.8 and 11.2 kcal/mol for β-lactoglobulin and albumin, respectively, compared to 5.1 kcal/mol in solution. Thus, both proteins protect trans-resveratrol from degradation, with albumin being more effective than β-lactoglobulin. The computational techniques clarify details of the binding of trans-resveratrol to the proteins and show that the stabilizing effect correlates with an increase of the dihedral order parameter of the ligand. These findings suggest that transport proteins are viable carriers to stabilize and deliver resveratrol in vivo in the biologically effective trans form.