Structural and anti-ovarian cancer insights into the immunoglobulin G-glabridin nanocomplex

In this study, the formation of the immunoglobulin G-glabridin (IgG-GB) complex and nanocomplex was analyzed by assessing the structure, stability, solubility, and anticancer effects against the human epithelial ovarian cancer cell line SKOV3. The hydrodynamic sizes of the prepared IgG-GB nanocomplex were 190.1 ± 25.68 nm (PDI: 0.19 ± 0.02), and the solubility levels of GB in the free and nanoformulated forms were 97.28 μg/mL and 368.95 ± 59.63 μg/mL, respectively. Additionally, the IgG-GB nanocomplex exhibited a slower and more sustained release of GB in a pH-sensitive manner. Spectroscopic measurements indicated logKb values of 4.01 and 4.66 for the IgG-GB complex and the IgG-GB nanocomplex, respectively. Furthermore, the main reaction type between IgG and GB was found to be hydrophobic forces, which led to the partial folding of IgG and nanoformulated IgG. Cellular assays demonstrated that the IC50 concentrations of GB, the IgG-GB complex, and the IgG-GB nanocomplex in ovarian cancer SKOV3 cells were 10.74, 10.05, and 6.39 μM, respectively, while these amounts were > 77.84 μM in normal epithelial FHC cells. Moreover, the IgG-GB nanocomplex resulted in increased membrane leakage, mitochondrial dysfunction, and upregulation of Bax/Bcl-2 and caspase-3, along with caspase-3 activity determined by LDH, MP, real-time PCR, and enzyme activity assays. In conclusion, an efficient IgG-GB nanocomplex was potentially prepared and developed as a selective anticancer system against ovarian cancer cells.