?-Lactoglobulin as a Nanotransporter for Glabridin: Exploring the Binding Properties and Bioactivity Influences.

ABSTRACT: Based on the fact that ?-lactoglobulin (?-lg) can solubilize readily in water and bind many small hydrophobic molecules, a novel nanocomplexed glabridin with ?-lg was developed by an antisolvent precipitation method. After binding to ?-lg, the solubility of glabridin in aqueous solution was enhanced 21 times. Fluorescence spectroscopy of ?-lg revealed that the interaction of glabridin with ?-lg made the environment of Trp and Tyr residues on ?-lg more hydrophilic. The morphology and crystal form of the nanocomplexed glabridin with ?-lg was characterized and the changes in ?-lg conformation was also been investigated. In combination with molecular docking modeling, the results revealed that glabridin was bound to ?-lg by hydrophobic forces and hydrogen-bond interactions. Furthermore, the nanocomplexed glabridin with ?-lg had a better 2,2-diphenyl-1-picrylhydrazyl radical-scavenging capacity and 2,2'-azino-bis-3-ethylbenzthiazoline-6-sulfonic acid radical-scavenging capacity compared to free glabridin at the same concentration during in vitro tests. Thus, nanocomplexing with ?-lg, by virtue of its ability to enhance the solubility of glabridin in aqueous systems, provides a suitable opportunity as a nanocarrier molecule.

SUBMITTER: Wei Y 

PROVIDER: S-EPMC6645583 | biostudies-literature | 2018 Sep

REPOSITORIES: biostudies-literature