Mechanistic Insights Into Protein Aggregation Inhibition by Green-Synthesized Silver Nanoparticles: A Study on Human...

Area of Science:

• Biomedical Nanotechnology
• Neurodegenerative Disease Research
• Protein Misfolding Disorders

Background:

• Neurodegenerative diseases like Alzheimer's and Parkinson's are characterized by amyloidogenic protein aggregation, lacking effective cures.
• Protein misfolding, triggered by aging or stress, leads to hazardous aggregate formation.
• Noble metal nanoparticles (NPs), particularly silver nanoparticles (AgNPs), offer unique properties for biomedical applications, including potential therapeutic roles.

Purpose of the Study:

• To develop biocompatible silver nanoparticles (AgNPs) using a green synthesis method.
• To investigate the chaperone-like activity of these AgNPs in inhibiting protein aggregation in vitro.
• To understand the mechanism of AgNP-mediated inhibition of human lysozyme (HLZ) aggregation.

Main Methods:

• Green synthesis of AgNPs using orange juice extract, followed by detailed characterization.
• In vitro assays using human lysozyme (HLZ) as a model protein to assess aggregation inhibition.
• Biophysical techniques including circular dichroism (CD), ANS fluorescence, ThT fluorescence, Congo red assay, and turbidity measurements were employed.

Main Results:

• Biogenic AgNPs demonstrated a concentration-dependent inhibition of HLZ aggregation, with an optimal effective concentration.
• Higher concentrations of AgNPs led to a decrease in inhibitory efficacy.
• Treatment of astrocytes with AgNPs resulted in reduced intracellular protein aggregation, indicating chaperone-like activity.

Conclusions:

• Green synthesized AgNPs possess significant chaperone-like activity against protein aggregation.
• These findings highlight the potential of biocompatible AgNPs as therapeutic agents for protein misfolding disorders.
• Further research into AgNP-mediated protein aggregation inhibition is warranted for neurodegenerative disease applications.