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Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids

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Published on: March 21, 2025

Modulating aβ33-42 peptide assembly by graphene oxide.

Qiang Li¹, Lei Liu, Shuai Zhang

¹Interdisciplinary Nanoscience Center (iNANO), Aarhus University, 8000 Aarhus C (Denmark), Fax: (+45) 8942-3690.

Chemistry (Weinheim an Der Bergstrasse, Germany)

|May 20, 2014

Summary

Graphene oxide modulates amyloid fibril formation by altering the assembly pathway of amyloid beta peptides. This suggests potential for graphene-based materials in inhibiting amyloidosis.

Keywords:

amyloid peptides assembly graphene oxide modulated structures

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Area of Science:

Biomaterials Science
Nanotechnology
Neuroscience

Background:

Amyloid fibrils are implicated in neurodegenerative diseases like Alzheimer's.
Controlling amyloid beta (Aβ) assembly is crucial for therapeutic development.
Graphene oxide (GO) possesses unique properties for biomolecular interaction.

Purpose of the Study:

To investigate the effect of graphene oxide (GO) on amyloid fibril (Aβ33-42) formation.
To explore GO's potential as a modulator for amyloid assembly pathways.
To assess the feasibility of graphene-based materials for inhibiting amyloidosis.

Main Methods:

Utilized graphene oxide (GO) as a modulator for amyloid fibril (Aβ33-42) formation.
Employed atomic force microscopy (AFM) for temporal evolution measurements.
Analyzed the initial binding interactions between peptide monomers and GO sheets.

Main Results:

Graphene oxide (GO) successfully tuned the formation and development of amyloid fibrils (Aβ33-42).
Atomic force microscopy revealed that GO redirects the amyloid beta assembly pathway.
Initial peptide monomer binding to GO surfaces significantly influences fibril formation.

Conclusions:

Graphene oxide acts as an effective modulator of amyloid beta assembly.
The interaction between GO and peptide monomers offers a strategy to control fibril formation.
Graphene-based materials show promise for developing novel inhibitors of amyloidosis.