Complexation of trans- and cis-resveratrol with bovine serum albumin, β-lactoglobulin or α-lactalbumin

By Hao Cheng, Z. Fang, Wusigale, A. M. Bakry, Yantao Chen, L. Liang. Food Hydrocolloids, 2018

103 citations recorded by the source corpus.

Abstract Clarification of the mechanism of protein-ligand interaction is important for the encapsulation of bioactive components. Trans -resveratrol is labile to convert to cis -isomer during fermentation and storage, but the cis -isomer interaction with proteins has not yet gained as much attention as that of trans -isomer. The influence of resveratrol's isomerization on interaction with ligand-binding proteins was investigated here. Cis -resveratrol exhibited higher affinity for bovine serum albumin than trans -isomer, but the isomerization to cis -isomer decreased the polyphenol affinity for α-lactalbumin and β-lactoglobulin. For each protein, trans - and cis -resveratrol shared the same optimal docking site but showed clear diversity in the second best site. Protein ternary complex could be formed when trans -/ cis -resveratrol were added in the sequence. Moreover, photostability of resveratrol and antioxidant activity of the polyphenol-protein mixtures were also discussed. The results gathered here should provide further insight into protein-polyphenol interactions and be useful for the development of protein-based carriers for the polyphenols.

Subfields: Biotechnology, Food Science, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/1ec1c19012d8bf97a636a6e122c0ec7bec3be2f4