1. Structure and biomedical applications of amyloid oligomer nanoparticles
- Author
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Ann-Kathrin Fuchs, Isabel Morgado, Oliver Ohlenschläger, Thomas Simmet, Erik Prell, Marcus Fändrich, Uwe Horn, Ramadurai Ramachandran, Senthil Kumar, Jay Kant Yadav, Matthias Görlach, Jessica Meinhardt, Jörg Leppert, Berthold Büchele, Tobias Aumüller, and Uwe Knüpfer
- Subjects
Amyloid ,Materials science ,Protein Conformation ,Neurodegeneration ,General Engineering ,Spheroid ,General Physics and Astronomy ,Nanoparticle ,medicine.disease ,Oligomer ,Nanomaterials ,chemistry.chemical_compound ,Biopolymers ,chemistry ,Biochemistry ,Microscopy, Electron, Transmission ,medicine ,Nanoparticles ,General Materials Science ,Protein folding ,Nuclear Magnetic Resonance, Biomolecular ,Iron oxide nanoparticles - Abstract
Amyloid oligomers are nonfibrillar polypeptide aggregates linked to diseases, such as Alzheimer's and Parkinson's. Here we show that these aggregates possess a compact, quasi-crystalline architecture that presents significant nanoscale regularity. The amyloid oligomers are dynamic assemblies and are able to release their individual subunits. The small oligomeric size and spheroid shape confer diffusible characteristics, electrophoretic mobility, and the ability to enter hydrated gel matrices or cells. We finally showed that the amyloid oligomers can be labeled with both fluorescence agents and iron oxide nanoparticles and can target macrophage cells. Oligomer amyloids may provide a new biological nanomaterial for improved targeting, drug release, and medical imaging.
- Published
- 2014