Amyloid-like bovine serum albumin fibrils as protein scaffold for biointerfaces

Amyloid-like protein assemblies have attracted increasing interest as bioinspired materials due to their structural stability and potential for interfacing with biological systems. In this study, the controlled conversion of bovine serum albumin (BSA) into amyloid-like fibrils and their potential use as biocompatible protein-based interfaces were investigated. The stability of BSA in different media was first evaluated by UV-Vis spectroscopy, demonstrating that the protein maintains its structural integrity over time and provides a suitable starting point for fibrillation experiments. Amyloid-like fibrils were subsequently generated under acidic and thermal conditions (pH 2 and 65 °C). A progressive decrease in α-helical content accompanied by an increase in β-sheet structures characteristic of amyloid assemblies was monitored by Furrier transform infrared (FTIR), Raman, and UV-Vis spectroscopy. The formation of fibrillar aggregates was further confirmed by Thioflavin T fluorescence analysis and atomic force microscopy (AFM), which showed the transition from globular protein aggregates to elongated fibrillar networks. AFM imaging also indicated that ionic strength influences fibril organization, with salt-containing media promoting the formation of more interconnected structures. Finally, the biological response of SH-SY5Y neuronal-like cells cultured on fibril-coated surfaces demonstrated enhanced cell attachment and spreading compared to non-modified substrates. Overall, the results highlight the potential of amyloid-like BSA fibrils as biocompatible protein-based scaffolds for the development of functional biointerfaces.