Cysteamine functionalized MoS₂ quantum dots inhibit amyloid aggregation.

Area of Science:

• Nanomaterials Science
• Biochemistry
• Materials Chemistry

Background:

• Amyloid fibrils, such as those formed by bovine serum albumin (BSA), are associated with various diseases.
• Developing effective inhibitors and therapeutic agents for amyloid-related diseases is a significant challenge.
• Molybdenum disulfide quantum dots (MoS₂ Qs) are emerging nanomaterials with potential biomedical applications.

Purpose of the Study:

• To synthesize cysteamine-functionalized MoS₂ QDs using a one-pot hydrothermal method.
• To investigate the efficacy of these MoS₂ QDs in inhibiting and reversing BSA amyloid fibrillation.
• To evaluate the biocompatibility and cytotoxicity of MoS₂ QDs in cellular models.

Main Methods:

• One-pot hydrothermal synthesis of cysteamine-functionalized MoS₂ QDs.
• Thioflavin T and 8-Anilino-1-naphthalenesulfonic acid fluorescence assays to monitor fibrillation.
• Circular dichroism and transmission electron microscopy to characterize fibrils and MoS₂ QDs.
• Methyl thiazolyl tetrazolium (MTT) assay to assess cytotoxicity in Hela cells.

Main Results:

• MoS₂ QDs effectively inhibited BSA fibrillogenesis and destabilized pre-formed BSA fibrils in a concentration-dependent manner.
• MoS₂ QDs demonstrated good biocompatibility, low toxicity, and effective cell penetration.
• MoS₂ QDs significantly reduced the cytotoxicity induced by BSA amyloid fibrils in Hela cells.

Conclusions:

• Cysteamine-functionalized MoS₂ QDs are promising agents for inhibiting and reversing amyloid fibrillation.
• These MoS₂ QDs exhibit favorable biocompatibility and possess therapeutic potential for amyloid-related diseases.
• This study provides insights into designing multifunctional nanomaterials for addressing amyloid pathologies.