Amyloid fibrils are polypeptide- or protein based supramolecules that are associated with serious diseases such as Alzheimer’s disease, type II diabetes or other misfolding disorders. Despite the physiological shortcomings, the assemblage of polypeptides and even proteins to supramolecular fibrils is a popular method for the generation of functional nanostructures and hybrid nanomaterials suited for applications in optoelectronic devices, nanosensors and actuators. The understanding of the molecular basis of the peptide monomer association process is the key to control fibrillation, which is necessary to develop potent modulators either in the medical or smart material field. It is well accepted that material surfaces influence the fibrillation process. For example, nanoparticles are considered as enhancers or suppressors.
An alanine-scan of N-terminal modified NNFGAIL peptides was conducted in order to examine the influence of the substituted amino acid position on the fibrillation time by Thioflavin-assays and DLS and the morphology by SEM. Moreover, the influence of metallic nanoparticles with different sizes and surface modifications on the fibrillation process of the peptides was examined. In addition to these characterization studies, the applicability of templated metallic nanoparticles synthesized by reduction using VUV-excimer radiation and immobilized on peptide fibrils as an electrode material in solid acid fuel cells was investigated as well as plasma treatment of the nanoparticle-fibril-assemblies.[4, 5]
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