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Luminophore Formation in Various Conformations of Bovine Serum Albumin by Binding of GoldIII
Published on: August 31, 2018
Modulation of bovine serum albumin aggregation by glutathione functionalized MoS2 quantum dots
Hua-Jin Zeng1, Li-Jun Sun2, Ling-Bo Qu2
1School of Pharmaceutical Sciences, Zhengzhou University, Zhengzhou 450001, PR China.
Abstract:
In present study, a novel glutathione functionalized MoS2 quantum dots (GSH-MoS2 QDs) was synthesized from sodium molybdate dehydrate and glutathione by using a one-pot hydrothermal method. After they were characterized, the influence of GSH-MoS2 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-MoS2 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-MoS2 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-MoS2 QDs is expected to become a candidate drug for the treatment of amyloid-related diseases.

