Cells proliferation on surfaces functionalized with amyloid beta peptide fibrils

Amyloid beta (Aβ) peptide aggregates are well-established biomarkers for Alzheimer's disease, though the complete etiology of this disorder remains elusive. Developing biointerfaces to elucidate the physiological roles of these peptides is essential. This study investigates the aggregation, fibrillation, and interaction of Aβ peptides with conductive, biocompatible nanostructured materials designed for applications involving neuronal cells. Various conductive, rigid, and flexible surfaces, both functionalized and non-functionalized with Aβ40 fibrils, were fabricated. These included glass substrates and poly(methyl methacrylate) electrospun fiber networks coated with gold via magnetron sputtering. The substrates were also functionalized through physical adsorption with poly-l-lysine and collagen, known to support cell proliferation, as well as with the inverse-Aβ40 peptide and an Amyloid Protein Non-Aβ Component, and the results were compared. The scaffolds were characterized using scanning electron microscopy, X-ray diffraction, atomic force microscopy, contact angle and electrical measurements, while their biological interactions were assessed using MTS assays, fluorescence imaging, and scanning electron microscopy. Fibroblast L929 and neuroblastoma SH-SY5Y cell lines were used as models, with results indicating an elevated cell viability, comparable to the control. The developed nanostructured surfaces are highly promising for integration into advanced neuromorphic engineering devices, as they have proven capable of maintaining their structural integrity when exposed to proteases.