The objective of the present contribution was to design and characterize resveratrol (RSV) and tocopherol (TOC) loaded 11S quinoa seed protein nanocomplexes. Firstly, molecular docking was performed to describe the probable binding sites between protein and ligands. Isothermal titration calorimetry allowed to obtain the thermodynamic parameters that described the molecular interactions between RSV or TOC with the protein. 11S globulin intrinsic fluorescence spectra showed a quenching effect exerted by RSV and TOC, demonstrating protein-bioactive compounds interactions. Stern-Volmer, Scatchard and Förster resonance energy transfer models application confirmed static quenching and allowed to obtain parameters that described the 11S-RSV or 11S-TOC complexation process. Secondly, protein aggregation induced by bioactive compounds interactions was confirmed by dynamic light scattering and atomic force microscopy with diameters <150 nm, detected by both techniques. Finally, it was found that antioxidant capacity of single 11S globulin did not decrease, meanwhile was additive for 11S-RSV. These nanocomplexes could constitute a real platform for the design of nutraceutical products.
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Rubinstein et al. (2024) studied this question.
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