Effect of 4-mercaptophenylboronic acid functionalized MoS quantum dots on amyloid aggregation of bovine serum albumin.

In recent years, seeking and screening of compounds that can inhibit and/or depolymerize protein aggregation has been a hot issue in the field of pharmaceutical research. As a new material, quantum dots have been widely concerned by medical researchers. In present study, a novel 4-mercaptophenylboronic acid functionalized MoS quantum dots (4-MPBA-MoS QDs) was successfully synthesized through a one-pot hydrothermal approach by using molybdate dehydrate and 4-mercaptophenylboronic acid as Mo and S source, respectively. Transmission electron microscopy observation showed that the morphology and microstructure of the 4-MPBA-MoS QDs displayed uniform spherical shape with a diameter of approximately 1.5 ∼ 3.0 nm. The UV and fluorescence spectra experiments indicated that the prepared QDs had good water solubility and two weak absorption peaks were appeared at 280 nm and 310 nm. When the excitation wavelength was set to 310 nm, the 4-MPBA-MoS QDs had the strongest fluorescence intensity, and the maximum emission wavelength appeared at 405 nm. In vitro experiments showed that the 4-MPBA-MoS QDs could significantly reduce the aggregation of bovine serum albumin (BSA). Especially when the mass ratio of BSA to 4-MPBA-MoS QDs was 1:5, the inhibition rate could reach 76.4%. Cell experiment showed that the presence of 4-MPBA-MoS QDs could obviously decrease the cytotoxicity induced by BSA amyloid fibrils. Moreover, the depolymerization of BSA amyloid fibrils by 4-MPBA-MoS QDs and its excellent cell permeability were also observed. Molecular docking studies have shown that 4-MPBA-MoS QDs may stabilize the BSA structure through van der Waals forces, hydrophobic force, electrostatic interactions and hydrogen bonds formed between the outer layer of 4-MPBA and BSA to prevent fibrosis aggregation. The results of this study suggested that 4-MPBA-MoS QDs showed low cytotoxicity, good biocompatibility and solubility, and had a great potential in the design of new drugs for the treatment of amyloid-related diseases.