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In present study, a novel glutathione functionalized MoS 2 quantum dots (GSH-MoS 2 QDs) was synthesized from sodium molybdate dehydrate and glutathione by using a one-pot hydrothermal method. After they were characterized, the influence of GSH-MoS 2 QDs on amyloid aggregation of bovine serum albumin (BSA) was investigated by various analytical methods including thioflavin T fluorescence assay, circular dichroism and transmission electron microscope. Moreover, the effect of GSH-MoS 2 QDs on cytotoxicity induced by BSA amyloid fibrils and cell penetration were evaluated by MTT assay and confocal fluorescence imaging, respectively. The results indicated that the GSH-MoS 2 QDs not only had good water solubility, excellent biocompatibility and low cytotoxicity, but also could obviously inhibit the aggregation of BSA and depolymerize the formed BSA aggregates. The data obtained from this work demonstrated that the GSH-MoS 2 QDs is expected to become a candidate drug for the treatment of amyloid-related diseases. • A novel GSH-MoS 2 QDs was synthesized by one-pot hydrothermal approach. • The as-prepared QDs can inhibit BSA aggregation and depolymerize BSA fibrils. • The QDs exhibits good biocompatibility, low cytotoxicity and cell permeability. [ABSTRACT FROM AUTHOR]

[Display omitted] • A novel 4-MPBA-MoS 2 QDs was synthesized by one-pot hydrothermal approach. • The prepared QDs have a uniform spherical appearance with a diameter of 1.5 ∼ 3.0 nm. • Inhibitory effects of the QDs on BSA amyloid aggregation were investigated. • Molecular docking reveals the mechanism of QDs inhibiting BSA amyloid aggregation. 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 2 quantum dots (4-MPBA-MoS 2 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 2 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 2 QDs had the strongest fluorescence intensity, and the maximum emission wavelength appeared at 405 nm. In vitro experiments showed that the 4-MPBA-MoS 2 QDs could significantly reduce the aggregation of bovine serum albumin (BSA). Especially when the mass ratio of BSA to 4-MPBA-MoS 2 QDs was 1:5, the inhibition rate could reach 76.4%. Cell experiment showed that the presence of 4-MPBA-MoS 2 QDs could obviously decrease the cytotoxicity induced by BSA amyloid fibrils. Moreover, the depolymerization of BSA amyloid fibrils by 4-MPBA-MoS 2 QDs and its excellent cell permeability were also observed. Molecular docking studies have shown that 4-MPBA-MoS 2 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 2 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. [ABSTRACT FROM AUTHOR]

In this study, the fibrillation of hen egg-white lysozyme (HEWL) in the absence and presence of different amount of nitrogen-doped graphene quantum dots (N-GQDs) was studied by Thioflavin T (ThT) spectroscopy, Congo red (CR) binding assays, 8-anilino-1-naphthalenesulfonic acid (ANS) fluorescence assay, circular dichroism (CD) and transmission electron microscopy (TEM). The experimental results indicated that not only the fibrillation of HEWL at high temperature (65 °C) and low pH (pH = 2.0) could be inhibited effectively by N-GQDs, but the inhibition of HEWL by N-GQDs followed a dose-dependent manner. The results of this work suggested that the N-GQDs had a great potential for designing new therapeutic agents and were promising for future treatment of amyloid-related diseases. [ABSTRACT FROM AUTHOR]