Nanoclay based study on protein stability and aggregation and its implication in human health

Area of Science:

• Biochemistry
• Materials Science
• Nanotechnology

Background:

• Protein aggregation is implicated in severe neurodegenerative and systemic amyloid diseases, including Alzheimer's, Parkinson's, and Type II Diabetes.
• Current treatments for these protein aggregation disorders are limited, necessitating novel therapeutic strategies.

Purpose of the Study:

• To investigate the potential of nanoclays as inhibitors of protein aggregation.
• To evaluate the efficacy of different nanoclays (MMT K-10, MMT K-30, Halloysite, Bentonite) in preventing the aggregation of Human Serum Albumin (HSA) and Human Lysozyme (HL).

Main Methods:

• Protein aggregation was induced and monitored using biophysical techniques: turbidity measurements, intrinsic fluorescence, ANS, Thioflavin T (Th T), Congo Red (CR) binding assays, and Circular Dichroism.
• The inhibitory effects of four types of nanoclays on HSA and HL aggregation were assessed.

Main Results:

• All tested nanoclays demonstrated inhibitory effects on DTT-induced protein aggregation.
• Bentonite and MMT K-10 exhibited the most significant and potent inhibition, notably by slowing the nucleation phase of aggregation.
• Biophysical assays confirmed the nanoclays' ability to interfere with the aggregation process.

Conclusions:

• Nanoclays can function as artificial chaperones, mitigating protein aggregation.
• Bentonite and MMT K-10 show promise as effective agents for developing treatments against protein aggregation-related disorders.
• This study highlights nanoclays as a potential therapeutic avenue for amyloid diseases.