Naringenin-Functionalized Gold Nanoparticles and Their Role in α-Synuclein Stabilization

Area of Science:

• Nanotechnology
• Neuroscience
• Biochemistry

Background:

• Protein misfolding and amyloid aggregation of intrinsically disordered proteins like alpha-synuclein are hallmarks of neurodegenerative diseases, including Parkinson's disease.
• Developing effective therapeutic strategies to prevent protein aggregation is crucial for treating these debilitating conditions.

Purpose of the Study:

• To synthesize and characterize naringenin-coated gold nanoparticles (NAR-AuNPs).
• To investigate the efficacy of NAR-AuNPs in inhibiting the aggregation of alpha-synuclein.
• To evaluate the potential of NAR-AuNPs as a therapeutic approach for Parkinson's disease.

Main Methods:

• One-pot synthesis of naringenin-coated gold nanoparticles (NAR-AuNPs).
• Characterization using dynamic light scattering, UV-Vis spectroscopy, zeta potential measurements, XPS, and FT-IR.
• Assessing the interaction of NAR-AuNPs with alpha-synuclein using spectroscopy and circular dichroism.
• Evaluating the cytotoxicity of NAR-AuNPs on neuronal cells.

Main Results:

• NAR-AuNPs were successfully synthesized with an average size of ~24 nm.
• The nanocomposite demonstrated strong interaction with alpha-synuclein, with a binding affinity in the micromolar range.
• NAR-AuNPs effectively inhibited alpha-synuclein conformational changes and prevented amyloid fibril formation.
• The naringenin-nanoparticle complex showed no adverse effects on neuronal cell viability.

Conclusions:

• Naringenin-embedded nanostructures (NAR-AuNPs) show significant potential in preventing alpha-synuclein aggregation.
• This approach offers a promising alternative strategy for developing treatments for Parkinson's disease and other protein conformation-related disorders.
• The biocompatibility and efficacy of NAR-AuNPs highlight their therapeutic promise.