Patterning amyloid peptide fibrils by AFM charge writing

Area of Science:

• Biomaterials Science
• Nanotechnology
• Surface Chemistry

Background:

• Amyloid fibrils have diverse applications but controlling their assembly on surfaces is challenging.
• Atomic force microscopy (AFM) enables nanoscale manipulation and surface characterization.
• Developing methods for precise patterning of biomolecules is crucial for advanced materials.

Purpose of the Study:

• To investigate the use of AFM-based surface charge patterns for directed assembly of peptide fibrils.
• To achieve controlled deposition of amyloid-like peptide fibrils with high lateral resolution.

Main Methods:

• Generating surface charge patterns on a polymethyl-methacrylate substrate using AFM-based charge writing.
• Encapsulating TTR105-115 peptide fibrils within water droplets in a water-in-perfluorocarbon oil emulsion.
• Observing the selective deposition of peptide fibrils onto the patterned charged surfaces.

Main Results:

• Achieved selective deposition of TTR105-115 peptide fibrils onto negatively charged patterns.
• Demonstrated a lateral resolution of approximately 1 micrometer for fibril patterning.
• Confirmed that peptide fibrils retained their rod morphology during the process.

Conclusions:

• AFM-based charge writing is an effective method for patterning amyloid-like peptide fibrils.
• This technique allows for precise control over the spatial arrangement of biomolecules on substrates.
• The findings open possibilities for creating novel nanostructured biomaterials.