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

Abstract

Based on the fact that β-lactoglobulin (β-lg) can solubilize readily in water and bind many small hydrophobic molecules, a novel nanocomplexed glabridin with β-lg was developed by an antisolvent precipitation method. After binding to β-lg, the solubility of glabridin in aqueous solution was enhanced 21 times. Fluorescence spectroscopy of β-lg revealed that the interaction of glabridin with β-lg made the environment of Trp and Tyr residues on β-lg more hydrophilic. The morphology and crystal form of the nanocomplexed glabridin with β-lg was characterized and the changes in β-lg conformation was also been investigated. In combination with molecular docking modeling, the results revealed that glabridin was bound to β-lg by hydrophobic forces and hydrogen-bond interactions. Furthermore, the nanocomplexed glabridin with β-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 β-lg, by virtue of its ability to enhance the solubility of glabridin in aqueous systems, provides a suitable opportunity as a nanocarrier molecule.

Investigating the Effect of the Azo Dye Amaranth on Beta Lactoglobulin by Multi-Spectroscopic Techniques and Molecular Docking: Role in Protein Aggregation

“…The binding constant K a and binding site values of and n were found to be 4.69 x 10 5 L mol -1 and 1.3, respectively, from the double logarithmic plot (Figure 2c). The n value suggests that there is a one-to-one interaction in the binding site of BLG, the binding constant values are on the order of 10 5 M −1 , and there is a strong binding affinity in the BLG-AMA complex (11) .…”

“…Measurements were taken at 282 nm with different AMA concentrations, where [Q] corresponds to the molar concentration of AMA. Based on the linear plot, it can be concluded that there is 1:1 complexation in the BLG-AMA system (11) . The binding constant K b was calculated to be 2.9 x 10 4 L mol -1 at pH 7.4 (298 K) by dividing the intercept by the slope (Figure 1 (c)).…”

“…The maximum emission wavelength of these amino acids is dependent on the hydrophobicity of the surrounding microenvironment. BLG exhibits fluorescence owing to the presence of two tryptophan and four tyrosine residues (11) . These aromatic amino acids contribute to the fluorescence of the protein.…”

“…Some azo dyes like Allura red, quinone yellow, and sunset yellow have been found to interact with proteins and induce protein aggregation (6,8,9) , which can have significant implications for various biological and biomedical processes. Amaranth may pose health risks, including its accumulation in the plasma and its interaction with human serum albumin, which can alter its secondary structure (10,11) . In a study conducted by Li et al, it was found that hydrophobic forces play a role in the formation of the complex between AMA and alpha-lactalbumin and amaranth has an impact on the conformation and functionality of alpha-lactalbumin, leading to modifications in its secondary structure (12) .…”

Phytochemicals Mediate Autophagy Against Osteoarthritis by Maintaining Cartilage Homeostasis

“…The clinical application of glabridin is limited due to its poor water solubility and therefore low bioavailability, but studies have shown that this situation can be improved by combining it with β -Lactoglobulin. ( Wei et al, 2018 ). These results indicate the potential of glabridin in OA prevention and treatment as a potential drug for OA.…”