Nanocellulose aerogels as 3D amyloid templates

Area of Science:

• Biomaterials Science
• Protein Chemistry
• Nanotechnology

Background:

• Proteins adsorb to surfaces, potentially forming amyloid structures, especially on nanoparticulate materials.
• Cellulose-based materials are explored as protein adsorption templates, but typically do not alter protein secondary structure.
• Previous work focused on inorganic or organic nanoparticles for amyloid templating.

Purpose of the Study:

• To investigate the use of bio-based TEMPO-oxidized cellulose nanofibers (TO-CNF) aerogels as three-dimensional templates for protein aggregation.
• To determine if TO-CNF aerogels can induce amyloid formation and alter protein aggregation kinetics.
• To explore the tuneable surface chemistry of TO-CNF aerogels for protein templating.

Main Methods:

• Utilized TEMPO-oxidized cellulose nanofibers (TO-CNF) to create three-dimensional aerogel templates.
• Applied a reducing agent, TCEP, in conjunction with TO-CNF aerogels to induce protein aggregation.
• Investigated protein adsorption, secondary structure changes, and bulk aggregation kinetics on TO-CNF aerogel surfaces.

Main Results:

• Induced the formation of amyloid-like protein 'worms' on TO-CNF aerogel surfaces with the aid of TCEP.
• Demonstrated that TO-CNF aerogels can induce bulk protein aggregation even when it previously did not occur.
• Showed that TO-CNF aerogels significantly increase the rate of 'worm' formation, reducing lag phases.

Conclusions:

• TO-CNF aerogels serve as effective bio-based templates for inducing ordered protein aggregation.
• These aerogels can promote amyloid formation and accelerate aggregation kinetics under specific conditions.
• The findings highlight the potential of cellulose-based aerogels in controlling protein self-assembly.