The team at Northwestern University develops engineered peptide amphiphile nanofibers that self-assemble through supramolecular polymerization to capture monomeric and oligomeric amyloid beta species. By incorporating bound Aβ42 into metastable nanostructures, the approach prevents neuronal uptake and maintains cell viability in vitro. This strategy targets early-stage soluble amyloid aggregates, offering a novel chemical tool to inhibit neurodegenerative processes associated with Alzheimer’s disease.
Key points
- Glycopeptide amphiphile nanofibers self-assemble via supramolecular copolymerization to form metastable structures that bind Aβ42 monomers and oligomers.
- Trehalose-functionalized peptides enhance nanofiber reactivity, physically entrapping soluble amyloid β42 and preventing neuronal uptake in iPSC-derived neuron cultures.
- Nanofiber treatment reduces Aβ-induced neuron death by over 60% in vitro, demonstrating cytoprotective efficacy against early Alzheimer’s pathogenesis.
Why it matters: Nanofiber trapping provides a chemical intervention to neutralize early soluble amyloid β, potentially transforming Alzheimer’s treatment at its source.
Q&A
- What are peptide amphiphiles?
- How do nanostructures block amyloid beta uptake?
- Why target soluble amyloid beta instead of plaques?
- What role does trehalose play in the nanofiber design?
- Can these nanofibers cross the blood-brain barrier?
